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"creatorSummary": "Browman et al.",
"parsedDate": "2007-08",
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"version": 1,
"itemType": "journalArticle",
"title": "The SPFH domain-containing proteins: more than lipid raft markers",
"creators": [
{
"creatorType": "author",
"firstName": "Duncan T",
"lastName": "Browman"
},
{
"creatorType": "author",
"firstName": "Maja B",
"lastName": "Hoegg"
},
{
"creatorType": "author",
"firstName": "Stephen M",
"lastName": "Robbins"
}
],
"abstractNote": "Membrane microdomains with distinct lipid compositions, called lipid rafts, represent a potential mechanism for compartmentalizing cellular functions within the plane of biological membranes. SPFH domain-containing proteins are found in lipid raft microdomains in diverse cellular membranes. The functions of these proteins are just beginning to be elucidated. Recent advances in the understanding of structural features and their roles within lipid rafts include a potential function for SPFH proteins in the formation of membrane microdomains and lipid raft-associated processes, such as endocytosis and mechanosensation.",
"publicationTitle": "Trends in Cell Biology",
"publisher": "",
"place": "",
"date": "Aug 2007",
"volume": "17",
"issue": "8",
"section": "",
"partNumber": "",
"partTitle": "",
"pages": "394-402",
"series": "",
"seriesTitle": "",
"seriesText": "",
"journalAbbreviation": "Trends Cell Biol",
"DOI": "10.1016/j.tcb.2007.06.005",
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"url": "http://www.ncbi.nlm.nih.gov/pubmed/17766116",
"accessDate": "2011-01-24T11:40:06Z",
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"shortTitle": "The SPFH domain-containing proteins",
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"callNumber": "",
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"extra": "PMID: 17766116",
"tags": [
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"type": 1
},
{
"tag": "Humans",
"type": 1
},
{
"tag": "Intracellular Signaling Peptides and Proteins",
"type": 1
},
{
"tag": "Membrane Microdomains",
"type": 1
},
{
"tag": "Membrane Proteins",
"type": 1
},
{
"tag": "Nerve Tissue Proteins",
"type": 1
},
{
"tag": "Protein Isoforms",
"type": 1
},
{
"tag": "Protein Structure, Tertiary",
"type": 1
},
{
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],
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"parsedDate": "2009-06-03",
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"data": {
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"version": 1,
"itemType": "journalArticle",
"title": "SLP-2 is required for stress-induced mitochondrial hyperfusion",
"creators": [
{
"creatorType": "author",
"firstName": "Daniel",
"lastName": "Tondera"
},
{
"creatorType": "author",
"firstName": "Stéphanie",
"lastName": "Grandemange"
},
{
"creatorType": "author",
"firstName": "Alexis",
"lastName": "Jourdain"
},
{
"creatorType": "author",
"firstName": "Mariusz",
"lastName": "Karbowski"
},
{
"creatorType": "author",
"firstName": "Yves",
"lastName": "Mattenberger"
},
{
"creatorType": "author",
"firstName": "Sébastien",
"lastName": "Herzig"
},
{
"creatorType": "author",
"firstName": "Sandrine",
"lastName": "Da Cruz"
},
{
"creatorType": "author",
"firstName": "Pascaline",
"lastName": "Clerc"
},
{
"creatorType": "author",
"firstName": "Ines",
"lastName": "Raschke"
},
{
"creatorType": "author",
"firstName": "Carsten",
"lastName": "Merkwirth"
},
{
"creatorType": "author",
"firstName": "Sarah",
"lastName": "Ehses"
},
{
"creatorType": "author",
"firstName": "Frank",
"lastName": "Krause"
},
{
"creatorType": "author",
"firstName": "David C",
"lastName": "Chan"
},
{
"creatorType": "author",
"firstName": "Christiane",
"lastName": "Alexander"
},
{
"creatorType": "author",
"firstName": "Christoph",
"lastName": "Bauer"
},
{
"creatorType": "author",
"firstName": "Richard",
"lastName": "Youle"
},
{
"creatorType": "author",
"firstName": "Thomas",
"lastName": "Langer"
},
{
"creatorType": "author",
"firstName": "Jean-Claude",
"lastName": "Martinou"
}
],
"abstractNote": "Mitochondria are dynamic organelles, the morphology of which results from an equilibrium between two opposing processes, fusion and fission. Mitochondrial fusion relies on dynamin-related GTPases, the mitofusins (MFN1 and 2) in the outer mitochondrial membrane and OPA1 (optic atrophy 1) in the inner mitochondrial membrane. Apart from a role in the maintenance of mitochondrial DNA, little is known about the physiological role of mitochondrial fusion. Here we report that mitochondria hyperfuse and form a highly interconnected network in cells exposed to selective stresses. This process precedes mitochondrial fission when it is triggered by apoptotic stimuli such as UV irradiation or actinomycin D. Stress-induced mitochondrial hyperfusion (SIMH) is independent of MFN2, BAX/BAK, and prohibitins, but requires L-OPA1, MFN1, and the mitochondrial inner membrane protein SLP-2. In the absence of SLP-2, L-OPA1 is lost and SIMH is prevented. SIMH is accompanied by increased mitochondrial ATP production and represents a novel adaptive pro-survival response against stress.",
"publicationTitle": "The EMBO Journal",
"publisher": "",
"place": "",
"date": "Jun 3, 2009",
"volume": "28",
"issue": "11",
"section": "",
"partNumber": "",
"partTitle": "",
"pages": "1589-1600",
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"journalAbbreviation": "EMBO J",
"DOI": "10.1038/emboj.2009.89",
"citationKey": "",
"url": "http://www.ncbi.nlm.nih.gov/pubmed/19360003",
"accessDate": "2011-01-12T12:46:45Z",
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"PMCID": "",
"ISSN": "1460-2075",
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"language": "",
"libraryCatalog": "NCBI PubMed",
"callNumber": "",
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"extra": "PMID: 19360003",
"tags": [
{
"tag": "Adenosine Triphosphate",
"type": 1
},
{
"tag": "Cells, Cultured",
"type": 1
},
{
"tag": "Dactinomycin",
"type": 1
},
{
"tag": "Fibroblasts",
"type": 1
},
{
"tag": "GTP Phosphohydrolases",
"type": 1
},
{
"tag": "Mice",
"type": 1
},
{
"tag": "Mitochondria",
"type": 1
},
{
"tag": "Stress, Physiological",
"type": 1
},
{
"tag": "Ultraviolet Rays",
"type": 1
}
],
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"creatorSummary": "Zhang et al.",
"parsedDate": "2004-11-09",
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"data": {
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"version": 1,
"itemType": "journalArticle",
"title": "MEC-2 is recruited to the putative mechanosensory complex in C. elegans touch receptor neurons through its stomatin-like domain",
"creators": [
{
"creatorType": "author",
"firstName": "Shifang",
"lastName": "Zhang"
},
{
"creatorType": "author",
"firstName": "Johanna",
"lastName": "Arnadottir"
},
{
"creatorType": "author",
"firstName": "Charles",
"lastName": "Keller"
},
{
"creatorType": "author",
"firstName": "Guy A",
"lastName": "Caldwell"
},
{
"creatorType": "author",
"firstName": "C Andrea",
"lastName": "Yao"
},
{
"creatorType": "author",
"firstName": "Martin",
"lastName": "Chalfie"
}
],
"abstractNote": "The response to gentle body touch in C. elegans requires a degenerin channel complex containing four proteins (MEC-2, MEC-4, MEC-6, and MEC-10). The central portion of the integral membrane protein MEC-2 contains a stomatin-like region that is highly conserved from bacteria to mammals. The molecular function of this domain in MEC-2, however, is unknown.\nHere, we show that MEC-2 colocalizes with the degenerin MEC-4 in regular puncta along touch receptor neuron processes. This punctate localization requires the other channel complex proteins. The stomatin-like region of MEC-2 interacts with the intracellular cytoplasmic portion of MEC-4. Missense mutations in this region that destroy the interaction also disrupt the punctate localization and degenerin-regulating function of MEC-2. Missense mutations outside this region apparently have no effect on the punctate localization but significantly reduce the regulatory effect of MEC-2 on the MEC-4 degenerin channel. A second stomatin-like protein, UNC-24, colocalizes with MEC-2 in vivo and coimmunoprecipitates with MEC-2 and MEC-4 in Xenopus oocytes; unc-24 enhances the touch insensitivity of temperature-sensitive alleles of mec-4 and mec-6.\nTwo stomatin homologs, MEC-2 and UNC-24, interact with the MEC-4 degenerin through their stomatin-like regions, which act as protein binding domains. At least in the case of MEC-2, this binding allows its nonstomatin domains to regulate channel activity. Stomatin-like regions in other proteins may serve a similar protein binding function.",
"publicationTitle": "Current Biology: CB",
"publisher": "",
"place": "",
"date": "Nov 9, 2004",
"volume": "14",
"issue": "21",
"section": "",
"partNumber": "",
"partTitle": "",
"pages": "1888-1896",
"series": "",
"seriesTitle": "",
"seriesText": "",
"journalAbbreviation": "Curr. Biol",
"DOI": "10.1016/j.cub.2004.10.030",
"citationKey": "",
"url": "http://www.ncbi.nlm.nih.gov/pubmed/15530389",
"accessDate": "2010-12-23T13:07:55Z",
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"PMCID": "",
"ISSN": "0960-9822",
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"language": "",
"libraryCatalog": "NCBI PubMed",
"callNumber": "",
"rights": "",
"extra": "PMID: 15530389",
"tags": [
{
"tag": "Alleles",
"type": 1
},
{
"tag": "Animals",
"type": 1
},
{
"tag": "Animals, Genetically Modified",
"type": 1
},
{
"tag": "Blotting, Western",
"type": 1
},
{
"tag": "Caenorhabditis elegans",
"type": 1
},
{
"tag": "Caenorhabditis elegans Proteins",
"type": 1
},
{
"tag": "Electrophysiology",
"type": 1
},
{
"tag": "Glutathione Transferase",
"type": 1
},
{
"tag": "Green Fluorescent Proteins",
"type": 1
},
{
"tag": "Immunohistochemistry",
"type": 1
},
{
"tag": "Immunoprecipitation",
"type": 1
},
{
"tag": "Mechanotransduction, Cellular",
"type": 1
},
{
"tag": "Membrane Proteins",
"type": 1
},
{
"tag": "Mutation, Missense",
"type": 1
},
{
"tag": "Protein Structure, Tertiary",
"type": 1
},
{
"tag": "Sensory Receptor Cells",
"type": 1
},
{
"tag": "Touch",
"type": 1
}
],
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"dateAdded": "2011-01-10T15:50:03Z",
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"creatorSummary": "Wetzel et al.",
"parsedDate": "2007-01-11",
"numChildren": 0
},
"data": {
"key": "IP7ZIWCI",
"version": 1,
"itemType": "journalArticle",
"title": "A stomatin-domain protein essential for touch sensation in the mouse",
"creators": [
{
"creatorType": "author",
"firstName": "Christiane",
"lastName": "Wetzel"
},
{
"creatorType": "author",
"firstName": "Jing",
"lastName": "Hu"
},
{
"creatorType": "author",
"firstName": "Dieter",
"lastName": "Riethmacher"
},
{
"creatorType": "author",
"firstName": "Anne",
"lastName": "Benckendorff"
},
{
"creatorType": "author",
"firstName": "Lena",
"lastName": "Harder"
},
{
"creatorType": "author",
"firstName": "Andreas",
"lastName": "Eilers"
},
{
"creatorType": "author",
"firstName": "Rabih",
"lastName": "Moshourab"
},
{
"creatorType": "author",
"firstName": "Alexey",
"lastName": "Kozlenkov"
},
{
"creatorType": "author",
"firstName": "Dominika",
"lastName": "Labuz"
},
{
"creatorType": "author",
"firstName": "Ombretta",
"lastName": "Caspani"
},
{
"creatorType": "author",
"firstName": "Bettina",
"lastName": "Erdmann"
},
{
"creatorType": "author",
"firstName": "Halina",
"lastName": "Machelska"
},
{
"creatorType": "author",
"firstName": "Paul A",
"lastName": "Heppenstall"
},
{
"creatorType": "author",
"firstName": "Gary R",
"lastName": "Lewin"
}
],
"abstractNote": "Touch and mechanical pain are first detected at our largest sensory surface, the skin. The cell bodies of sensory neurons that detect such stimuli are located in the dorsal root ganglia, and subtypes of these neurons are specialized to detect specific modalities of mechanical stimuli. Molecules have been identified that are necessary for mechanosensation in invertebrates but so far not in mammals. In Caenorhabditis elegans, mec-2 is one of several genes identified in a screen for touch insensitivity and encodes an integral membrane protein with a stomatin homology domain. Here we show that about 35% of skin mechanoreceptors do not respond to mechanical stimuli in mice with a mutation in stomatin-like protein 3 (SLP3, also called Stoml3), a mammalian mec-2 homologue that is expressed in sensory neurons. In addition, mechanosensitive ion channels found in many sensory neurons do not function without SLP3. Tactile-driven behaviours are also impaired in SLP3 mutant mice, including touch-evoked pain caused by neuropathic injury. SLP3 is therefore indispensable for the function of a subset of cutaneous mechanoreceptors, and our data support the idea that this protein is an essential subunit of a mammalian mechanotransducer.",
"publicationTitle": "Nature",
"publisher": "",
"place": "",
"date": "Jan 11, 2007",
"volume": "445",
"issue": "7124",
"section": "",
"partNumber": "",
"partTitle": "",
"pages": "206-209",
"series": "",
"seriesTitle": "",
"seriesText": "",
"journalAbbreviation": "Nature",
"DOI": "10.1038/nature05394",
"citationKey": "",
"url": "http://www.ncbi.nlm.nih.gov/pubmed/17167420",
"accessDate": "2010-12-23T13:10:12Z",
"PMID": "",
"PMCID": "",
"ISSN": "1476-4687",
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"shortTitle": "",
"language": "",
"libraryCatalog": "NCBI PubMed",
"callNumber": "",
"rights": "",
"extra": "PMID: 17167420",
"tags": [
{
"tag": "Afferent Pathways",
"type": 1
},
{
"tag": "Animals",
"type": 1
},
{
"tag": "Electric Conductivity",
"type": 1
},
{
"tag": "Female",
"type": 1
},
{
"tag": "Ganglia, Spinal",
"type": 1
},
{
"tag": "Male",
"type": 1
},
{
"tag": "Mechanoreceptors",
"type": 1
},
{
"tag": "Membrane Proteins",
"type": 1
},
{
"tag": "Mice",
"type": 1
},
{
"tag": "Mutation",
"type": 1
},
{
"tag": "Nerve Tissue Proteins",
"type": 1
},
{
"tag": "Protein Structure, Tertiary",
"type": 1
},
{
"tag": "Rats",
"type": 1
},
{
"tag": "Sodium Channels",
"type": 1
},
{
"tag": "Touch",
"type": 1
}
],
"collections": [],
"relations": {},
"dateAdded": "2011-01-10T15:50:03Z",
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"version": 1,
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"creatorSummary": "Tavernarakis et al.",
"parsedDate": "1999-11",
"numChildren": 0
},
"data": {
"key": "IXFEQHTQ",
"version": 1,
"itemType": "journalArticle",
"title": "The SPFH domain: implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins",
"creators": [
{
"creatorType": "author",
"firstName": "N",
"lastName": "Tavernarakis"
},
{
"creatorType": "author",
"firstName": "M",
"lastName": "Driscoll"
},
{
"creatorType": "author",
"firstName": "N C",
"lastName": "Kyrpides"
}
],
"abstractNote": "",
"publicationTitle": "Trends in Biochemical Sciences",
"publisher": "",
"place": "",
"date": "Nov 1999",
"volume": "24",
"issue": "11",
"section": "",
"partNumber": "",
"partTitle": "",
"pages": "425-427",
"series": "",
"seriesTitle": "",
"seriesText": "",
"journalAbbreviation": "Trends Biochem. Sci",
"DOI": "",
"citationKey": "",
"url": "http://www.ncbi.nlm.nih.gov/pubmed/10542406",
"accessDate": "2010-12-27T18:57:45Z",
"PMID": "",
"PMCID": "",
"ISSN": "0968-0004",
"archive": "",
"archiveLocation": "",
"shortTitle": "The SPFH domain",
"language": "",
"libraryCatalog": "NCBI PubMed",
"callNumber": "",
"rights": "",
"extra": "PMID: 10542406",
"tags": [
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"abstractNote": "Membrane protein - microvilli - lipid raft - GPI-anchored protein - epithelial cell The 31 kDa integral membrane protein stomatin (protein 7.2b) has a monotopic structure and a cytofacial orientation. We have shown previously that stomatin is located in plasma membrane protruding structures and forms high-order homo-oligomers in the human epithelial cell line UAC, suggesting that this protein has a structural function in the cortical morphogenesis of the cells. It is also present in a pool of juxtanuclear vesicles. In this study, we show that stomatin colocalizes with the GPI-anchored proteins placental alkaline phosphatase (PLAP) and membrane folate receptor alpha (MFRalpha) endogenously expressed in UAC cells. This observation enabled us to demonstrate two different aspects of stomatin. First, using anti-PLAP antibody internalization, we show that the peri-centrosomal vesicles containing stomatin correspond to a subset of endosomes, which can also be labeled with the late endosomal/lysosomal marker LAMP-2. Secondly, we found that stomatin is partially present in detergent-insoluble membrane domains and co-patches with PLAP on the plasma membrane, after cross-linking of PLAP by antibodies. These data indicate that stomatin and GPI-anchored proteins are linked through lipid rafts and undergo the same sorting events. We propose that stomatin, through its affinity for lipid rafts, functions in concentrating GPI-anchored proteins in membrane microvillar structures. Consistent with this hypothesis, we found that stomatin is expressed exclusively in microvilli of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells.",
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"title": "Cysteine 29 is the major palmitoylation site on stomatin",
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"abstractNote": "The 31 kDa membrane protein stomatin was metabolically labeled with tritiated palmitic acid in the human amniotic cell line UAC and immunoprecipitated. We show that the incorporated palmitate is sensitive to hydroxylamine, indicating the binding to cysteine residues. Stomatin contains three cysteines. By expressing a myc-tagged stomatin and substituting the three cysteines by serine, individually or in combination, we demonstrate that Cys-29 is the predominant site of palmitoylation and that Cys-86 accounts for the remaining palmitate labeling. Disruption of Cys-52 alone does not show any detectable reduction of palmitic acid incorporation. Given the organization of stomatin into homo-oligomers, the presence of multiple palmitate chains is likely to increase greatly the affinity of these oligomers for the membrane and perhaps particular lipid domains within it.",
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"title": "Oligomeric nature of the integral membrane protein stomatin",
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"abstractNote": "The 31-kDa integral membrane protein stomatin (protein 7.2b) is not only an important component of the red cell membrane but can also be found in abundance in different tissues and cell lines. The protein is thought to be anchored to the membrane by a hydrophobic domain while both N and C termini are exposed to the cytoplasm. We have previously shown in the human cell line UAC that stomatin concentrates preferentially in plasma membrane folds and protrusions. There is also evidence that stomatin is linked to the cortical actin cytoskeleton, suggesting a role in cortical morphogenesis of the cell. In this study, we demonstrate that the fundamental structure of stomatin is oligomeric. Whereas interaction of stomatin with itself was suggested by cross-linking experiments, we show by density gradient centrifugation analysis that soluble homo-oligomeric complexes of this protein are present in Triton X-100 extracts of UAC cells. We also show the existence of these oligomers by co-immunoprecipitation of the endogenous stomatin and a recombinantly expressed myc-tagged stomatin, using an anti-myc antibody. The data indicate that these complexes comprise between 9 and 12 monomers of stomatin. Two C-terminally truncated forms of stomatin do not incorporate into these oligomers, suggesting an involvement of the C terminus in the homo-oligomeric interaction.",
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"title": "Podocin participates in the assembly of tight junctions between foot processes in nephrotic podocytes",
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"firstName": "Akemi",
"lastName": "Shono"
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{
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"firstName": "Hidetake",
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"firstName": "Xiao-Song",
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"abstractNote": "The predominant type of cellular junction between normal podocyte foot processes is the slit diaphragm. Under nephrotic conditions,however, foot process effacement leads to the loss of slit diaphragms and the new formationof tight junctions composed of the proteins coxsackievirus and adenovirus receptor (CAR) and zonula occludens 1 (ZO-1). Podocin, a protein that plays a key role in maintaining the integrity of the slit diaphragm, has also been localized to these tight junctions, but its function at this site is unknown. In this study, we confirmed that podocin colocalizes with CAR and ZO-1 at the tight junction between foot processes in nephrotic rats. Using primary cultures of rat podocytes, as well as cell lines that co-expressed podocin and CAR, we observed that podocin was recruited to sites of cell-cell contact and that it co-localized with CAR and ZO-1. Immunoprecipitation suggested that these three junctional proteins from a multi-protein complex. Consistent with this, we found that podociin facilitated the coalescence of preassembled lipid rafts containing CAR and restricted their lateral mobility, the latter likely a result of dynamic actin reorganization and subsequent tethering of CAR-podocin complexes to the cytoskeleton. In conclusion, in addition to serving as a structural protein of the slit diaphragm of normal podocytes, our data suggest that podocin may also serve as a scaffold that links tight junction proteins to the actin cytoskeleton in nephrotic foot processes.",
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{
"creatorType": "author",
"firstName": "Tilman",
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{
"creatorType": "author",
"firstName": "David G",
"lastName": "Camp"
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{
"creatorType": "author",
"firstName": "Uwe",
"lastName": "Ahting"
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{
"creatorType": "author",
"firstName": "Thomas",
"lastName": "Waizenegger"
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{
"creatorType": "author",
"firstName": "Curt",
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{
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"firstName": "Axel",
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{
"creatorType": "author",
"firstName": "Walter",
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{
"creatorType": "author",
"firstName": "Peter J",
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{
"creatorType": "author",
"firstName": "Doron",
"lastName": "Rapaport"
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"abstractNote": "The mitochondrial outer membrane mediates numerous interactions between the metabolic and genetic systems of mitochondria and the rest of the eukaryotic cell. We performed a proteomic study to discover novel functions of components of the mitochondrial outer membrane. Proteins of highly pure outer membrane vesicles (OMV) from Neurospora crassa were identified by a combination of LC-MS/MS of tryptic peptide digests and gel electrophoresis of solubilized OMV proteins, followed by their identification using MALDI-MS PMF. Among the 30 proteins found in at least three of four separate analyses were 23 proteins with known functions in the outer membrane. These included components of the import machinery (the TOM and TOB complexes), a pore-forming component (porin), and proteins that control fusion and fission of the organelle. In addition, proteins playing a role in various biosynthetic pathways, whose intracellular location had not been established previously, could be localized to the mitochondrial outer membrane. Thus, the proteome of the outer membrane can help in identifying new mitochondria-related functions.",
"publicationTitle": "Proteomics",
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"abstractNote": "Band 7 membrane protein was metabolically labelled with [32P]phosphate in the presence of cAMP, isolated and digested, the labelled peptides were purified and sequenced. Ser-9 was identified as the only phosphorylation site. This proves that the N-terminal region is located at the cytoplasmic side of the membrane and implies a monotopic rather than the predicted bitopic structure.",
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"firstName": "Cédric",
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"firstName": "Jean-Luc",
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{
"creatorType": "author",
"firstName": "Jean",
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"abstractNote": "Of all cells, human erythrocytes express the highest level of the Glut1 glucose transporter. However, the regulation and function of Glut1 during erythropoiesis are not known. Here, we report that glucose transport actually decreases during human erythropoiesis despite a >3-log increase in Glut1 transcripts. In contrast, Glut1-mediated transport of L-dehydroascorbic acid (DHA), an oxidized form of ascorbic acid (AA), is dramatically enhanced. We identified stomatin, an integral erythrocyte membrane protein, as regulating the switch from glucose to DHA transport. Notably though, we found that erythrocyte Glut1 and associated DHA uptake are unique traits of humans and the few other mammals that have lost the ability to synthesize AA from glucose. Accordingly, we show that mice, a species capable of synthesizing AA, express Glut4 but not Glut1 in mature erythrocytes. Thus, erythrocyte-specific coexpression of Glut1 with stomatin constitutes a compensatory mechanism in mammals that are unable to synthesize vitamin C.",
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"creatorType": "author",
"firstName": "Anne G",
"lastName": "Benckendorff"
},
{
"creatorType": "author",
"firstName": "Li-Yang",
"lastName": "Chiang"
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{
"creatorType": "author",
"firstName": "Rui",
"lastName": "Wang"
},
{
"creatorType": "author",
"firstName": "Nevena",
"lastName": "Milenkovic"
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{
"creatorType": "author",
"firstName": "Christiane",
"lastName": "Wetzel"
},
{
"creatorType": "author",
"firstName": "Jing",
"lastName": "Hu"
},
{
"creatorType": "author",
"firstName": "Cheryl L",
"lastName": "Stucky"
},
{
"creatorType": "author",
"firstName": "Marilyn G",
"lastName": "Parra"
},
{
"creatorType": "author",
"firstName": "Narla",
"lastName": "Mohandas"
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{
"creatorType": "author",
"firstName": "Gary R",
"lastName": "Lewin"
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"abstractNote": "Somatic sensory neurons of the dorsal root ganglia are necessary for a large part of our mechanosensory experience. However, we only have a good knowledge of the molecules required for mechanotransduction in simple invertebrates such as the nematode Caenorhabiditis elegans. In C. elegans, a number of so-called mec genes have been isolated that are required for the transduction of body touch. One such gene, mec-2 codes for an integral membrane protein of the stomatin family, a large group of genes with a stomatin homology domain. Using stomatin null mutant mice, we have tested the hypothesis that the founding member of this family, stomatin might play a role in the transduction of mechanical stimuli by primary sensory neurons. We used the in vitro mouse skin nerve preparation to record from a large population of low- and high-threshold mechanoreceptors with myelinated A-fiber (n = 553) and unmyelinated C-fiber (n = 157) axons. One subtype of mechanoreceptor, the d-hair receptor, which is a rapidly adapting mechanoreceptor, had reduced sensitivity to mechanical stimulation in the absence of stomatin. Other cutaneous mechanoreceptors, including nociceptive C-fibers were not affected by the absence of a functional stomatin protein. Patch-clamp analysis of presumptive D-hair receptor mechanoreceptive neurons, which were identified by a characteristic rosette morphology in culture, showed no change in membrane excitability in the absence of the stomatin protein. We conclude that stomatin is required for normal mechanotransduction in a subpopulation of vertebrate sensory neurons.",
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"firstName": "Ko",
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"creatorType": "author",
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"lastName": "Hayashi"
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{
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"lastName": "Morita"
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"creatorType": "author",
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"lastName": "Huber"
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"abstractNote": "Stomatin is an integral membrane protein which is widely expressed in many cell types. It is accepted that stomatin has a unique hairpin-loop topology: it is anchored to the membrane with an N-terminal hydrophobic domain and the N- and C-termini are cytoplasmically localized. Stomatin is a prototype for a family of related proteins, containing among others MEC-2 (mechanosensory protein 2) from Caenorhabditis elegans, SLP (stomatin-like protein)-3 and podocin, all of which interact with ion channels to regulate their activity. Members of the stomatin family partly localize in DRMs (detergent-resistant membrane domains) enriched in cholesterol and sphingolipids. It has been proposed that a highly conserved proline residue in the middle of the hydrophobic domain directly binds cholesterol and that cholesterol binding is necessary for the regulation of ion channels. In the present study we show that a small part of the stomatin pool exists as a single-pass transmembrane protein rather than a hairpin-loop protein. The highly conserved proline residue is crucial for adopting the hairpin-loop topology: substitution of this proline residue by serine transfers the whole stomatin pool to the single-pass transmembrane form, which no longer localizes to DRMs. These results suggest that formation of the hairpin loop is inefficient and that the conserved proline residue is indispensable for formation of the hairpin loop. The single-pass transmembrane form exists also for SLP-3 and it should be considered that it mediates part of the physiological functions of stomatin and related proteins.",
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"journalAbbreviation": "Biochem. J",
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"title": "A stomatin-like protein necessary for mechanosensation in C. elegans",
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"creatorType": "author",
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{
"creatorType": "author",
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{
"creatorType": "author",
"firstName": "E L",
"lastName": "Ferguson"
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{
"creatorType": "author",
"firstName": "M",
"lastName": "Chalfie"
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"abstractNote": "The mec-2 gene is required for the function of a set of six touch receptor neurons in the nematode Caenorhabditis elegans; mec-2 mutants, which are touch-insensitive, have touch cells that appear morphologically normal. Gene interaction studies suggest that mec-2 positively regulates the activity of the putative mechanosensory transduction channel (and the present paper), comprised in part of proteins encoded by the two degenerin genes mec-4 and mec-10 The central region of the mec-2 protein (MEC-2) is very similar to stomatin, an integral membrane protein (band 7.2b) in human red blood cells that is thought to regulate cation conductance. MEC-2-LacZ fusions are distributed along the touch receptor axons. This axonal distribution, which is mediated by the mec-2-specific amino terminus, is disrupted by mutations in mec-12, an alpha-tubulin gene needed for touch cell function. Our results indicate that MEC-2 links the mechanosensory channel and the microtubule cytoskeleton of the touch receptor neurons. Such linkage provides the basis for a mechanism of mechanosensation whereby microtubule displacement leads to channel opening.",
"publicationTitle": "Nature",
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"date": "Nov 16, 1995",
"volume": "378",
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"pages": "292-295",
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"creatorType": "author",
"firstName": "C M",
"lastName": "Hiebl-Dirschmied"
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"lastName": "Entler"
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"firstName": "C",
"lastName": "Stratowa"
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"creatorType": "author",
"firstName": "R",
"lastName": "Prohaska"
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"abstractNote": "cDNA clones encoding the human erythrocyte band 7 membrane protein were isolated by immunoscreening from bone marrow and HeLa cell lambda gt 11 cDNA libraries, and their nucleotide sequences were determined. HeLa- and bone marrow cell-derived sequences were identical, except for one nucleotide; the deduced sequence of 287 amino acids was confirmed by sequence identity with peptides of the erythroid protein. Structure analysis assigned band 7 protein to the type Ib transmembrane proteins.",
"publicationTitle": "Biochimica Et Biophysica Acta",
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"date": "Aug 27, 1991",
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"title": "Isolation and partial characterization of the human erythrocyte band 7 integral membrane protein",
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"creatorType": "author",
"firstName": "C M",
"lastName": "Hiebl-Dirschmied"
},
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"creatorType": "author",
"firstName": "G R",
"lastName": "Adolf"
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"creatorType": "author",
"firstName": "R",
"lastName": "Prohaska"
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],
"abstractNote": "Monoclonal antibodies to the Mr 31,000 major integral membrane protein of the human erythrocyte band 7 region were used to identify the corresponding polypeptide chain and epitope-carrying fragments on immunoblots. Analysis of the erythrocyte membrane, membrane fractions, and cytosol revealed that the Mr 31,000 band 7 integral membrane protein is unique and not related to any of the other water-soluble or membrane-bound band 7 components. Cross-reacting proteins were identified in the membranes of other mammalian erythrocytes and in cell lines of epithelial and lymphoid origin. Proteolytic digestion of intact human erythrocytes or erythrocyte membranes demonstrated that the band 7 integral membrane protein has an intracellular domain larger than Mr 12,000; it does not have an extracellular one. One of the monoclonal antibodies was employed for the isolation of band 7 integral membrane protein by immunoaffinity chromatography; subsequent Edman degradation revealed a blocked N-terminus.",
"publicationTitle": "Biochimica Et Biophysica Acta",
"publisher": "",
"place": "",
"date": "Jun 18, 1991",
"volume": "1065",
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"url": "http://www.ncbi.nlm.nih.gov/pubmed/1711899",
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"creatorSummary": "Hájek et al.",
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"title": "Identification of a novel mitochondrial complex containing mitofusin 2 and stomatin-like protein 2",
"creators": [
{
"creatorType": "author",
"firstName": "Petr",
"lastName": "Hájek"
},
{
"creatorType": "author",
"firstName": "Anne",
"lastName": "Chomyn"
},
{
"creatorType": "author",
"firstName": "Giuseppe",
"lastName": "Attardi"
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],
"abstractNote": "A reverse genetics approach was utilized to discover new proteins that interact with the mitochondrial fusion mediator mitofusin 2 (Mfn2) and that may participate in mitochondrial fusion. In particular, in vivo formaldehyde cross-linking of whole HeLa cells and immunoprecipitation with purified Mfn2 antibodies of SDS cell lysates were used to detect an approximately 42-kDa protein. This protein was identified by liquid chromatography and tandem mass spectrometry as stomatin-like protein 2 (Stoml2), previously described as a peripheral plasma membrane protein of unknown function associated with the cytoskeleton of erythrocytes (Wang, Y., and Morrow, J. S. (2000) J. Biol. Chem. 275, 8062-8071). Immunoblot analysis with anti-Stoml2 antibodies showed that Stoml2 could be immunoprecipitated specifically with Mfn2 antibody either from formaldehyde-cross-linked and SDS-lysed cells or from cells lysed with digitonin. Subsequent immunocytochemistry and cell fractionation experiments fully supported the conclusion that Stoml2 is indeed a mitochondrial protein. Furthermore, demonstration of mitochondrial membrane potential-dependent import of Stoml2 accompanied by proteolytic processing, together with the results of sublocalization experiments, suggested that Stoml2 is associated with the inner mitochondrial membrane and faces the intermembrane space. Notably, formaldehyde cross-linking revealed a \"ladder\" of high molecular weight protein species, indicating the presence of high molecular weight Stoml2-Mfn2 hetero-oligomers. Knockdown of Stoml2 by the short interfering RNA approach showed a reduction of the mitochondrial membrane potential, without, however, any obvious changes in mitochondrial morphology.",
"publicationTitle": "The Journal of Biological Chemistry",
"publisher": "",
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"date": "Feb 23, 2007",
"volume": "282",
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"journalAbbreviation": "J. Biol. Chem",
"DOI": "10.1074/jbc.M608168200",
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"itemType": "journalArticle",
"title": "Slipins: ancient origin, duplication and diversification of the stomatin protein family",
"creators": [
{
"creatorType": "author",
"firstName": "Jasper B",
"lastName": "Green"
},
{
"creatorType": "author",
"firstName": "J Peter W",
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],
"abstractNote": "Stomatin is a membrane protein that was first isolated from human red blood cells. Since then, a number of stomatin-like proteins have been identified in all three domains of life. The conservation among these proteins is remarkable, with bacterial and human homologs sharing 50 % identity. Despite being associated with a variety of diseases such as cancer, kidney failure and anaemia, precise functions of these proteins remain unclear.\nWe have constructed a comprehensive phylogeny of all 'stomatin-like' sequences that share a 150 amino acid domain. We show these proteins comprise an ancient family that arose early in prokaryotic evolution, and we propose a new nomenclature that reflects their phylogeny, based on the name \"slipin\" (stomatin-like protein). Within prokaryotes there are two distinct subfamilies that account for the two different origins of the eight eukaryotic stomatin subfamilies, one of which gave rise to eukaryotic SLP-2, renamed here \"paraslipin\". This was apparently acquired through the mitochondrial endosymbiosis and is widely distributed amongst the major kingdoms. The other prokaryotic subfamily gave rise to the ancestor of the remaining seven eukaryotic subfamilies. The highly diverged \"alloslipin\" subfamily is represented only by fungal, viral and ciliate sequences. The remaining six subfamilies, collectively termed \"slipins\", are confined to metazoa. Protostome stomatin, as well as a newly reported arthropod subfamily slipin-4, are restricted to invertebrate groups, whilst slipin-1 (previously SLP-1) is present in nematodes and higher metazoa. In vertebrates, the stomatin family expanded considerably, with at least two duplication events giving rise to podocin and slipin-3 subfamilies (previously SLP-3), with the retained ancestral sequence giving rise to vertebrate stomatin.\nStomatin-like proteins have their origin in an ancient duplication event that occurred early on in the evolution of prokaryotes. By constructing a phylogeny of this family, we have identified and named a number of orthologous groups: these can now be used to infer function of stomatin subfamilies in a meaningful way.",
"publicationTitle": "BMC Evolutionary Biology",
"publisher": "",
"place": "",
"date": "2008",
"volume": "8",
"issue": "",
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"partTitle": "",
"pages": "44",
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"seriesTitle": "",
"seriesText": "",
"journalAbbreviation": "BMC Evol. Biol",
"DOI": "10.1186/1471-2148-8-44",
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"url": "http://www.ncbi.nlm.nih.gov/pubmed/18267007",
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"itemType": "journalArticle",
"title": "MEC-2 regulates C. elegans DEG/ENaC channels needed for mechanosensation",
"creators": [
{
"creatorType": "author",
"firstName": "Miriam B",
"lastName": "Goodman"
},
{
"creatorType": "author",
"firstName": "Glen G",
"lastName": "Ernstrom"
},
{
"creatorType": "author",
"firstName": "Dattananda S",
"lastName": "Chelur"
},
{
"creatorType": "author",
"firstName": "Robert",
"lastName": "O'Hagan"
},
{
"creatorType": "author",
"firstName": "C Andrea",
"lastName": "Yao"
},
{
"creatorType": "author",
"firstName": "Martin",
"lastName": "Chalfie"
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],
"abstractNote": "Touch sensitivity in animals relies on nerve endings in the skin that convert mechanical force into electrical signals. In the nematode Caenorhabditis elegans, gentle touch to the body wall is sensed by six mechanosensory neurons that express two amiloride-sensitive Na+ channel proteins (DEG/ENaC). These proteins, MEC-4 and MEC-10, are required for touch sensation and can mutate to cause neuronal degeneration. Here we show that these mutant or 'd' forms of MEC-4 and MEC-10 produce a constitutively active, amiloride-sensitive ionic current when co-expressed in Xenopus oocytes, but not on their own. MEC-2, a stomatin-related protein needed for touch sensitivity, increased the activity of mutant channels about 40-fold and allowed currents to be detected with wild-type MEC-4 and MEC-10. Whereas neither the central, stomatin-like domain of MEC-2 nor human stomatin retained the activity of full-length MEC-2, both produced amiloride-sensitive currents with MEC-4d. Our findings indicate that MEC-2 regulates MEC-4/MEC-10 ion channels and raise the possibility that similar ion channels may be formed by stomatin-like proteins and DEG/ENaC proteins that are co-expressed in both vertebrates and invertebrates. Some of these channels may mediate mechanosensory responses.",
"publicationTitle": "Nature",
"publisher": "",
"place": "",
"date": "Feb 28, 2002",
"volume": "415",
"issue": "6875",
"section": "",
"partNumber": "",
"partTitle": "",
"pages": "1039-1042",
"series": "",
"seriesTitle": "",
"seriesText": "",
"journalAbbreviation": "Nature",
"DOI": "10.1038/4151039a",
"citationKey": "",
"url": "http://www.ncbi.nlm.nih.gov/pubmed/11875573",
"accessDate": "2010-12-23T13:03:17Z",
"PMID": "",
"PMCID": "",
"ISSN": "0028-0836",
"archive": "",
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"language": "",
"libraryCatalog": "NCBI PubMed",
"callNumber": "",
"rights": "",
"extra": "PMID: 11875573",
"tags": [
{
"tag": "Amiloride",
"type": 1
},
{
"tag": "Animals",
"type": 1
},
{
"tag": "Blood Proteins",
"type": 1
},
{
"tag": "Caenorhabditis elegans",
"type": 1
},
{
"tag": "Caenorhabditis elegans Proteins",
"type": 1
},
{
"tag": "Electrophysiology",
"type": 1
},
{
"tag": "Epithelial Sodium Channel",
"type": 1
},
{
"tag": "Escherichia coli",
"type": 1
},
{
"tag": "Genes, Helminth",
"type": 1
},
{
"tag": "Helminth Proteins",
"type": 1
},
{
"tag": "Humans",
"type": 1
},
{
"tag": "Ion Channels",
"type": 1
},
{
"tag": "Mechanoreceptors",
"type": 1
},
{
"tag": "Membrane Proteins",
"type": 1
},
{
"tag": "Mutation",
"type": 1
},
{
"tag": "Oocytes",
"type": 1
},
{
"tag": "Protein Structure, Tertiary",
"type": 1
},
{
"tag": "Recombinant Proteins",
"type": 1
},
{
"tag": "Sodium",
"type": 1
},
{
"tag": "Sodium Channels",
"type": 1
},
{
"tag": "Touch",
"type": 1
},
{
"tag": "Xenopus",
"type": 1
}
],
"collections": [],
"relations": {},
"dateAdded": "2011-01-10T15:50:03Z",
"dateModified": "2011-01-10T15:50:03Z"
}
},
{
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"version": 1,
"library": {
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"creatorSummary": "Gallagher and Forget",
"parsedDate": "1995-11-03",
"numChildren": 0
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"version": 1,
"itemType": "journalArticle",
"title": "Structure, organization, and expression of the human band 7.2b gene, a candidate gene for hereditary hydrocytosis",
"creators": [
{
"creatorType": "author",
"firstName": "P G",
"lastName": "Gallagher"
},
{
"creatorType": "author",
"firstName": "B G",
"lastName": "Forget"
}
],
"abstractNote": "Band 7.2b is an integral membrane phosphoprotein absent from the erythrocyte membranes of patients with hereditary hydrocytosis, a hemolytic anemia inherited in an autosomal dominant fashion and characterized by stomatocytic red blood cells with abnormal permeability to Na+ and K+. The precise role of band 7.2b is unknown, but it may interact with other proteins of the junctional complex of the membrane skeleton. To gain additional insight into the structure and function of this protein and to provide the necessary tools for further genetic studies of hydrocytosis patients, we determined the sequence of the full-length human band 7.2b cDNA, characterized the genomic structure of the band 7.2b gene, studied its pattern of expression in different tissues, and characterized the promoter of the gene. The composite band 7.2b gene cDNA was 3047 base pairs in length. Northern blot analysis revealed a wide tissue distribution of expression of the band 7.2b gene, with utilization of alternative polyadenylation signals generating transcripts of 2.2 and 3.1 kilobases. Cloning of the band 7.2b chromosomal gene revealed that it is composed of seven exons distributed over 40 kilobases of DNA. The band 7.2b gene promoter was identified as a TATA-less, (G+C)-rich promoter with a typical InR recognition sequence and a single transcription initiation site. It directed high level expression of a reporter gene in both erythroid and nonerythroid cells. An imperfect simple sequence repeat polymorphism was identified in the 5'-flanking DNA, and an assay was developed for its analysis by PCR.",
"publicationTitle": "The Journal of Biological Chemistry",
"publisher": "",
"place": "",
"date": "Nov 3, 1995",
"volume": "270",
"issue": "44",
"section": "",
"partNumber": "",
"partTitle": "",
"pages": "26358-26363",
"series": "",
"seriesTitle": "",
"seriesText": "",
"journalAbbreviation": "J. Biol. Chem",
"DOI": "",
"citationKey": "",
"url": "http://www.ncbi.nlm.nih.gov/pubmed/7592848",
"accessDate": "2010-12-26T11:40:02Z",
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"PMCID": "",
"ISSN": "0021-9258",
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"extra": "PMID: 7592848",
"tags": [
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"type": 1
},
{
"tag": "Amino Acid Sequence",
"type": 1
},
{
"tag": "Anemia, Hemolytic",
"type": 1
},
{
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"type": 1
},
{
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"type": 1
},
{
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"type": 1
},
{
"tag": "Blotting, Northern",
"type": 1
},
{
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"type": 1
},
{
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"type": 1
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"type": 1
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{
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"type": 1
},
{
"tag": "Genetic Variation",
"type": 1
},
{
"tag": "Hominidae",
"type": 1
},
{
"tag": "Humans",
"type": 1
},
{
"tag": "Introns",
"type": 1
},
{
"tag": "Leukemia, Erythroblastic, Acute",
"type": 1
},
{
"tag": "Membrane Proteins",
"type": 1
},
{
"tag": "Mice",
"type": 1
},
{
"tag": "Molecular Sequence Data",
"type": 1
},
{
"tag": "Polymerase Chain Reaction",
"type": 1
},
{
"tag": "Polymorphism, Genetic",
"type": 1
},
{
"tag": "Promoter Regions, Genetic",
"type": 1
},
{
"tag": "RNA, Messenger",
"type": 1
},
{
"tag": "Recombinant Fusion Proteins",
"type": 1
},
{
"tag": "Regulatory Sequences, Nucleic Acid",
"type": 1
},
{
"tag": "Restriction Mapping",
"type": 1
},
{
"tag": "Transfection",
"type": 1
},
{
"tag": "Tumor Cells, Cultured",
"type": 1
}
],
"collections": [],
"relations": {},
"dateAdded": "2011-01-10T15:50:03Z",
"dateModified": "2011-01-10T15:50:03Z"
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"version": 1,
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"creatorSummary": "Da Cruz et al.",
"parsedDate": "2010-01",
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"version": 1,
"itemType": "journalArticle",
"title": "SLP-2 negatively modulates mitochondrial sodium-calcium exchange",
"creators": [
{
"creatorType": "author",
"firstName": "Sandrine",
"lastName": "Da Cruz"
},
{
"creatorType": "author",
"firstName": "Umberto",
"lastName": "De Marchi"
},
{
"creatorType": "author",
"firstName": "Maud",
"lastName": "Frieden"
},
{
"creatorType": "author",
"firstName": "Philippe A",
"lastName": "Parone"
},
{
"creatorType": "author",
"firstName": "Jean-Claude",
"lastName": "Martinou"
},
{
"creatorType": "author",
"firstName": "Nicolas",
"lastName": "Demaurex"
}
],
"abstractNote": "Mitochondria play a major role in cellular calcium homeostasis. Despite decades of studies, the molecules that mediate and regulate the transport of calcium ions in and out of the mitochondrial matrix remain unknown. Here, we investigate whether SLP-2, an inner membrane mitochondrial protein of unknown function, modulates the activity of mitochondrial Ca(2+) transporters. In HeLa cells depleted of SLP-2, the amplitude and duration of mitochondrial Ca(2+) elevations evoked by agonists were decreased compared to control cells. SLP-2 depletion increased the rates of calcium extrusion from mitochondria. This effect disappeared upon Na(+) removal or addition of CGP-37157, an inhibitor of the mitochondrial Na(+)/Ca(2+) exchanger, and persisted in permeabilized cells exposed to a fixed cytosolic Na(+) and Ca(2+) concentration. The rates of mitochondrial Ca(2+) extrusion were prolonged in SLP-2 over-expressing cells, independently of the amplitude of mitochondrial Ca(2+) elevations. The amplitude of cytosolic Ca(2+) elevations was increased by SLP-2 depletion and decreased by SLP-2 over-expression. These data show that SLP-2 modulates mitochondrial calcium extrusion, thereby altering the ability of mitochondria to buffer Ca(2+) and to shape cytosolic Ca(2+) signals.",
"publicationTitle": "Cell Calcium",
"publisher": "",
"place": "",
"date": "Jan 2010",
"volume": "47",
"issue": "1",
"section": "",
"partNumber": "",
"partTitle": "",
"pages": "11-18",
"series": "",
"seriesTitle": "",
"seriesText": "",
"journalAbbreviation": "Cell Calcium",
"DOI": "10.1016/j.ceca.2009.10.005",
"citationKey": "",
"url": "http://www.ncbi.nlm.nih.gov/pubmed/19944461",
"accessDate": "2010-12-25T16:46:09Z",
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"PMCID": "",
"ISSN": "1532-1991",
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"shortTitle": "",
"language": "",
"libraryCatalog": "NCBI PubMed",
"callNumber": "",
"rights": "",
"extra": "PMID: 19944461",
"tags": [
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"type": 1
},
{
"tag": "Calcium",
"type": 1
},
{
"tag": "Calcium Signaling",
"type": 1
},
{
"tag": "Clonazepam",
"type": 1
},
{
"tag": "Cytosol",
"type": 1
},
{
"tag": "Hela Cells",
"type": 1
},
{
"tag": "Humans",
"type": 1
},
{
"tag": "Membrane Proteins",
"type": 1
},
{
"tag": "Mitochondria",
"type": 1
},
{
"tag": "Mitochondrial Membranes",
"type": 1
},
{
"tag": "RNA, Small Interfering",
"type": 1
},
{
"tag": "Sodium",
"type": 1
},
{
"tag": "Sodium-Calcium Exchanger",
"type": 1
},
{
"tag": "Thiazepines",
"type": 1
}
],
"collections": [],
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"dateAdded": "2011-01-10T15:50:03Z",
"dateModified": "2011-01-10T15:50:03Z"
}
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]