1998
DOI: 10.1016/s0378-1119(98)00532-0
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Molecular cloning of hSLP-1, a novel human brain-specific member of the band 7/MEC-2 family similar to Caenorhabditis elegans UNC-24

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Cited by 45 publications
(41 citation statements)
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“…Nonspecific lipid transport proteins serve as intracellular carriers of cholesterol and other sterols, so the association of a similar domain with a cholesterol-binding PHB domain is suggestive that the two domains shuttle cholesterol and other sterols into the plasma membrane. 40,42 In contrast to MEC-2 and UNC-24, MEC-6 has a single membrane-spanning domain that puts most of the protein on the extracellular side of the membrane. 39 The similarity of MEC-6 with paraoxonases may indicate that it, too, affects the cholesterol content of the membrane, albeit at the outer leaflet of the bilayer, because two of the three vertebrate paraoxonases are secreted and associated with cholesterol-containing HDL particles.…”
Section: Palmitoylation Regulates Interaction With Cholesterolmentioning
confidence: 99%
“…Nonspecific lipid transport proteins serve as intracellular carriers of cholesterol and other sterols, so the association of a similar domain with a cholesterol-binding PHB domain is suggestive that the two domains shuttle cholesterol and other sterols into the plasma membrane. 40,42 In contrast to MEC-2 and UNC-24, MEC-6 has a single membrane-spanning domain that puts most of the protein on the extracellular side of the membrane. 39 The similarity of MEC-6 with paraoxonases may indicate that it, too, affects the cholesterol content of the membrane, albeit at the outer leaflet of the bilayer, because two of the three vertebrate paraoxonases are secreted and associated with cholesterol-containing HDL particles.…”
Section: Palmitoylation Regulates Interaction With Cholesterolmentioning
confidence: 99%
“…Stomatin, or band 7.2b, was first identified as a membrane-associated protein in erythrocytes, and is thought to be involved in cation channel regulation (Gallagher and Forget 1995;Stewart et al 1992;Hiebl-Dirschmied et al 1991); however, its definitive function remains to be elucidated (Delaunay et al 1999;Zhu et al 1999). The stomatin family includes stomatin-like-protein 1 (SLP1), SLP2, and podocin (Boute et al 2000;Wang and Morrow 2000;Seidel and Prohaska 1998), as well as homologs in zebrafish, Caenorhabditis elegans, Drosophila, and plants (Rajaram et al 1998;Huang et al 1995). We have designated this newly identified protein stomatin-like-protein 3 (SLP3), in accordance with the published nomenclature for the gene family.…”
Section: Slp3: a Novel Member Of The Stomatin Gene Familymentioning
confidence: 99%
“…Recently, stomatin has also been shown to be expressed in mechanosensory neurons, where it may interact directly with transduction components, including cation channels (Goodman et al 2002;Fricke et al 2000;Mannsfeldt et al 1999). Other stomatin family members-SLP1, SLP2, and NPHS2 (podocin)-also display selective expression patterns (Boute et al 2000;Wang and Morrow 2000;Seidel and Prohaska 1998). For instance, robust SLP1 expression appears to be restricted to brain, with low-level expression detectable in heart and skeletal muscle, while podocin expression is restricted to renal glomeruli.…”
Section: Introductionmentioning
confidence: 99%
“…Furthermore, stomatin was shown to interact with acid-sensing ion channels and to alter their gating in mammalian cells [17]. Stomatins are the founding members of a family of proteins called stomatin-like proteins which include SLP-1, 2 and 3 [18,19]. A function has not yet been ascribed to these three proteins but it is known that SLP-2 is expressed in a range of mammalian tissues, notably the plasma membrane of erythrocytes [20].…”
Section: Introductionmentioning
confidence: 99%