Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain

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dc.contributor.authorNielsen, E.en
dc.contributor.authorChristoforidis, S.en
dc.contributor.authorUttenweiler-Joseph, S.en
dc.contributor.authorMiaczynska, M.en
dc.contributor.authorDewitte, F.en
dc.contributor.authorWilm, M.en
dc.contributor.authorHoflack, B.en
dc.contributor.authorZerial, M.en
dc.date.accessioned2015-11-24T18:55:15Z
dc.date.available2015-11-24T18:55:15Z
dc.identifier.issn0021-9525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/18842
dc.rightsDefault Licence-
dc.subjectAmino Acid Motifsen
dc.subjectAmino Acid Sequenceen
dc.subjectCarrier Proteins/*chemistry/genetics/*metabolismen
dc.subjectCathepsin D/metabolismen
dc.subjectCell Lineen
dc.subjectCloning, Molecularen
dc.subjectEndosomes/chemistry/*metabolismen
dc.subjectFluorescent Antibody Techniqueen
dc.subjectHeLa Cellsen
dc.subjectHumansen
dc.subjectLysosomes/chemistry/metabolismen
dc.subjectMembrane Fusionen
dc.subjectMembrane Microdomains/chemistry/metabolismen
dc.subjectMembrane Proteins/chemistry/genetics/*metabolismen
dc.subjectMolecular Sequence Dataen
dc.subjectMunc18 Proteinsen
dc.subjectNerve Tissue Proteins/chemistryen
dc.subjectPhosphatidylinositol 3-Kinases/metabolismen
dc.subjectProtein Bindingen
dc.subjectProtein Processing, Post-Translationalen
dc.subjectProtein Structure, Tertiaryen
dc.subjectProtein Transporten
dc.subjectQa-SNARE Proteinsen
dc.subjectSequence Alignmenten
dc.subjectSequence Homology, Amino Aciden
dc.subjectTransfectionen
dc.subject*Vesicular Transport Proteinsen
dc.subjectrab5 GTP-Binding Proteins/*metabolismen
dc.titleRabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domainen
heal.abstractRab5 regulates endocytic membrane traffic by specifically recruiting cytosolic effector proteins to their site of action on early endosomal membranes. We have characterized a new Rab5 effector complex involved in endosomal fusion events. This complex includes a novel protein, Rabenosyn-5, which, like the previously characterized Rab5 effector early endosome antigen 1 (EEA1), contains an FYVE finger domain and is recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. Rabenosyn-5 is complexed to the Sec1-like protein hVPS45. hVPS45 does not interact directly with Rab5, therefore Rabenosyn-5 serves as a molecular link between hVPS45 and the Rab5 GTPase. This property suggests that Rabenosyn-5 is a closer mammalian functional homologue of yeast Vac1p than EEA1. Furthermore, although both EEA1 and Rabenosyn-5 are required for early endosomal fusion, only overexpression of Rabenosyn-5 inhibits cathepsin D processing, suggesting that the two proteins play distinct roles in endosomal trafficking. We propose that Rab5-dependent formation of membrane domains enriched in phosphatidylinositol-3-phosphate has evolved as a mechanism for the recruitment of multiple effector proteins to mammalian early endosomes, and that these domains are multifunctional, depending on the differing activities of the effector proteins recruited.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/11062261-
heal.identifier.secondaryhttp://jcb.rupress.org/content/151/3/601.full.pdf-
heal.journalNameJ Cell Biolen
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate2000-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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