Phosphorylation of a membrane curvature-sensing motif switches function of the HOPS subunit Vps41 in membrane tethering

DC FieldValueLanguage
dc.contributor.authorCabrera, Margarita
dc.contributor.authorLangemeyer, Lars
dc.contributor.authorMari, Muriel
dc.contributor.authorRethmeier, Ralf
dc.contributor.authorOrban, Ioan
dc.contributor.authorPerz, Angela
dc.contributor.authorBrocker, Cornelia
dc.contributor.authorGriffith, Janice
dc.contributor.authorKlose, Daniel
dc.contributor.authorSteinhoff, Heinz Jurgen
dc.contributor.authorReggiori, Fulvio
dc.contributor.authorVandre, Siegfried Engelbrecht
dc.contributor.authorUngermann, Christian
dc.date.accessioned2021-12-23T16:13:01Z-
dc.date.available2021-12-23T16:13:01Z-
dc.date.issued2010
dc.identifier.issn00219525
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/10366-
dc.description.abstractTethering factors are organelle specific multisubunit protein complexes that identify, along with Rab guanosine iriphosphatases, transport vesicles and trigger their SNARE mediated fusion of specific transport vesicles with the target membranes Little is known about how tethering factors discriminate between different trafficking pathways, which may converge at the same organelle In this paper, we describe a phosphorylation based switch mechanism, which allows the homotypic vacuole fusion protein sorting effector subunit Vps41 to operate in two distinct fusion events, namely endosome vacuole and AP 3 vesicle-vacuole fusion Vps41 contains an amphipathic lipid-packing sensor (ALPS) motif, which recognizes highly curved membranes At endosomes, this motif is inserted into the lipid bilayer and masks the binding motif for the 8 subunit of the AP 3 complex, Apl5, without affecting the Vps41 function in endosome vacuole fusion At the much less curved vacuole, the ALPS motif becomes available for phosphorylation by the resident casein kinase Yck3 As a result, the Apl5-binding site is exposed and allows AP-3 vesicles to bind to Vps41, followed by specific fusion with the vacuolar membrane This multi functional tethering factor thus discriminates between trafficking routes by switching from a curvature sensing to a coat recognition mode upon phosphorylation
dc.description.sponsorshipHans Muhlenhoff Foundation; Netherlands Organization for Health Research and Development (ZonMW)Netherlands Organization for Health Research and Development [917 76 329]; Utrecht University; [Sonderforschungsbereich 431]; This work was supported by the Sonderforschungsbereich 431 the Hans Muhlenhoff Foundation (grant to C Ungermann) the Netherlands Organization for Health Research and Development (grant ZonMW VIDI 917 76 329) and the Utrecht University (High Potential grant to F Reggion)
dc.language.isoen
dc.publisherROCKEFELLER UNIV PRESS
dc.relation.ispartofJOURNAL OF CELL BIOLOGY
dc.subjectCell Biology
dc.subjectCOMPLEX
dc.subjectCRYOSECTIONING PROCEDURE
dc.subjectDOCKING
dc.subjectENDOCYTIC COMPARTMENTS
dc.subjectHOMOLOG
dc.subjectPROTEIN
dc.subjectT-SNARE
dc.subjectULTRASTRUCTURAL ANALYSIS
dc.subjectVACUOLE FUSION
dc.subjectYEAST SACCHAROMYCES-CEREVISIAE
dc.titlePhosphorylation of a membrane curvature-sensing motif switches function of the HOPS subunit Vps41 in membrane tethering
dc.typejournal article
dc.identifier.doi10.1083/jcb.201004092
dc.identifier.isiISI:000284737200016
dc.description.volume191
dc.description.issue4
dc.description.startpage845
dc.description.endpage859
dc.contributor.orcid0000-0002-2978-8255
dc.contributor.orcid0000-0002-2978-8255
dc.contributor.orcid0000-0002-5888-0157
dc.contributor.orcid0000-0002-3597-0889
dc.contributor.orcid0000-0002-4309-0910
dc.contributor.orcid0000-0002-2677-6945
dc.contributor.orcid0000-0003-2652-2686
dc.contributor.researcheridU-8327-2019
dc.contributor.researcheridF-3306-2016
dc.contributor.researcheridY-1225-2019
dc.contributor.researcheridH-3791-2014
dc.publisher.place1114 FIRST AVE, 4TH FL, NEW YORK, NY 10021 USA
dcterms.isPartOf.abbreviationJ. Cell Biol.
dcterms.oaStatusGreen Submitted, Green Published, hybrid
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptidfb04-
crisitem.author.deptidfb04-
crisitem.author.orcid0000-0002-3597-0889-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidKlDa004-
crisitem.author.netidStHe633-
crisitem.author.netidUnCh999-
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