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dc.creatorFernández-Chacón, Rafael 
dc.creatorSüdhof, Thomas C. 
dc.date.accessioned2015-01-19T11:12:24Z
dc.date.available2015-01-19T11:12:24Z
dc.date.issued2000
dc.identifier.issn1529-2401es
dc.identifier.issn0270-6474es
dc.identifier.urihttp://hdl.handle.net/11441/17817
dc.description.abstractIn vertebrates, secretory carrier membrane proteins (SCAMPs) 1–3 constitute a family of putative membrane-trafficking proteins composed of cytoplasmic N-terminal sequences with NPF repeats, four central transmembrane regions (TMRs), and a cytoplasmic tail. SCAMPs probably function in endocytosis by recruiting EH-domain proteins to the N-terminal NPF repeats but may have additional functions mediated by their other sequences. We now demonstrate that SCAMPs form a much larger and more heterogeneous protein family than envisioned previously, with an evolutionary conservation extending to invertebrates and plants. Two novel vertebrate SCAMPs (SCAMPs 4 and 5), single SCAMP genes in Caenorhabditis elegans and Drosophila melanogaster, and multiple SCAMPs in Arabidopsis thaliana were identified. Interestingly, the novel SCAMPs 4 and 5 lack the N-terminal NPF repeats that are highly conserved in all other SCAMPs. RNA and Western blotting experiments showed that SCAMPs 1–4 are ubiquitously coexpressed, whereas SCAMP 5 is only detectable in brain where it is expressed late in development coincident with the elaboration of mature synapses. Immunocytochemistry revealed that SCAMP 5 exhibits a synaptic localization, and subcellular fractionations demonstrated that SCAMP 5 is highly enriched in synaptic vesicles. Our studies characterize SCAMPs as a heterogeneous family of putative trafficking proteins composed of three isoforms that are primarily synthesized outside of neurons (SCAMPs 2–4), one isoform that is ubiquitously expressed but highly concentrated on synaptic vesicles (SCAMP 1), and one brain-specific isoform primarily localized to synaptic vesicles (SCAMP 5). The conservation of the TMRs in all SCAMPs with the variable presence of N-terminal NPF repeats suggests that in addition to the role of some SCAMPs in endocytosis mediated by their NPF repeats, all SCAMPs perform a “core” function in membrane traffic mediated by their TMRs.es
dc.language.isoenges
dc.relation.ispartofThe Journal of Neuroscience, November 1, 2000, 20(21):7941–7950en
dc.relation.ispartofJournal of neuroscience, 20 (21), 7941-7950.es
dc.rightsAtribución-NoComercial-SinDerivadas 4.0 España*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectsynaptic vesicleses
dc.subjectexocytosises
dc.subjectendocytosises
dc.subjectclathrines
dc.subjecttransport vesicle buddinges
dc.subjectintersectines
dc.subjectEH domaines
dc.titleNovel SCAMPs Lacking NPF Repeats: Ubiquitous and Synaptic Vesicle-Specific Forms Implicate SCAMPs in Multiple Membrane- Trafficking Functionses
dc.typeinfo:eu-repo/semantics/articlees
dc.rights.accessrightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Fisiología Médica y Biofísicaes
dc.journaltitleJournal of neurosciencees
dc.publication.volumen20es
dc.publication.issue21es
dc.publication.initialPage7941es
dc.publication.endPage7950es
dc.identifier.idushttps://idus.us.es/xmlui/handle/11441/17817

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Except where otherwise noted, this item's license is described as: Atribución-NoComercial-SinDerivadas 4.0 España