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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/18842
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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.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/11062261-
heal.identifier.secondaryhttp://jcb.rupress.org/content/151/3/601.full.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2000-
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.journalNameJ Cell Biolen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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