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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/123456789/22417
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dc.contributor.authorVitale, G.en
dc.contributor.authorRybin, V.en
dc.contributor.authorChristoforidis, S.en
dc.contributor.authorThornqvist, P.en
dc.contributor.authorMcCaffrey, M.en
dc.contributor.authorStenmark, H.en
dc.contributor.authorZerial, M.en
dc.date.accessioned2015-11-24T19:24:06Z-
dc.date.available2015-11-24T19:24:06Z-
dc.identifier.issn0261-4189-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/22417-
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectCattleen
dc.subjectCell Lineen
dc.subjectCricetinaeen
dc.subjectCytosol/chemistryen
dc.subjectDimerizationen
dc.subjectEndosomes/metabolismen
dc.subjectGTP-Binding Proteins/analysis/*metabolismen
dc.subjectGuanosine Triphosphate/*metabolismen
dc.subjectHeLa Cellsen
dc.subjectHumansen
dc.subjectMembrane Proteins/analysis/chemistry/genetics/*metabolismen
dc.subjectMolecular Sequence Dataen
dc.subjectProtein Bindingen
dc.subjectProtein Structure, Secondaryen
dc.subjectRecombinant Fusion Proteinsen
dc.subjectSequence Alignmenten
dc.subject*Vesicular Transport Proteinsen
dc.subjectrab4 GTP-Binding Proteinsen
dc.subjectrab5 GTP-Binding Proteinsen
dc.titleDistinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5en
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1093/emboj/17.7.1941-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/9524117-
heal.identifier.secondaryhttp://www.nature.com/emboj/journal/v17/n7/pdf/7590907a.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1998-
heal.abstractRabaptin-5 functions as an effector for the small GTPase Rab5, a regulator of endocytosis and early endosome fusion. We have searched for structural determinants that confer functional specificity on Rabaptin-5. Here we report that native cytosolic Rabaptin-5 is present in a homodimeric state and dimerization depends upon the presence of its coiled-coil predicted sequences. A 73 residue C-terminal region of Rabaptin-5 is necessary and sufficient both for the interaction with Rab5 and for Rab5-dependent recruitment of the protein on early endosomes. Surprisingly, we uncovered the presence of an additional Rab-binding domain at the N-terminus of Rabaptin-5. This domain mediates the direct interaction with the GTP-bound form of Rab4, a small GTPase that has been implicated in recycling from early endosomes to the cell surface. Based on these results, we propose that Rabaptin-5 functions as a molecular linker between two sequentially acting GTPases to coordinate endocytic and recycling traffic.en
heal.journalNameEMBO Jen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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