Vps41 Phosphorylation and the Rab Ypt7 Control the Targeting of the HOPS Complex to Endosome-Vacuole Fusion Sites
DC Element | Wert | Sprache |
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dc.contributor.author | Cabrera, Margarita | |
dc.contributor.author | Ostrowicz, Clemens W. | |
dc.contributor.author | Mari, Muriel | |
dc.contributor.author | LaGrassa, Tracy J. | |
dc.contributor.author | Reggiori, Fulvio | |
dc.contributor.author | Ungermann, Christian | |
dc.date.accessioned | 2021-12-23T16:13:42Z | - |
dc.date.available | 2021-12-23T16:13:42Z | - |
dc.date.issued | 2009 | |
dc.identifier.issn | 10591524 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/10701 | - |
dc.description.abstract | Membrane fusion depends on multisubunit tethering factors such as the vacuolar HOPS complex. We previously showed that the vacuolar casein kinase Yck3 regulates vacuole biogenesis via phosphorylation of the HOPS subunit Vps41. Here, we link the identified Vps41 phosphorylation site to HOPS function at the endosome-vacuole fusion site. The nonphosphorylated Vps41 mutant (Vps41 S-A) accumulates together with other HOPS subunits on punctate structures proximal to the vacuole that expand in a class E mutant background and that correspond to in vivo fusion sites. Ultrastructural analysis of this mutant confirmed the presence of tubular endosomal structures close to the vacuole. In contrast, Vps41 with a phosphomimetic mutation (Vps41 S-D) is mislocalized and leads to multilobed vacuoles, indicative of a fusion defect. These two phenotypes can be rescued by overproduction of the vacuolar Rab Ypt7, revealing that both Ypt7 and Yck3-mediated phosphorylation modulate the Vps41 localization to the endosome-vacuole junction. Our data suggest that Vps41 phosphorylation fine-tunes the organization of vacuole fusion sites and provide evidence for a fusion ``hot spot'' on the vacuole limiting membrane. | |
dc.description.sponsorship | Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [SFB431, CA806/2-1]; Fundacion Ramon Areces; Hans-Muhlen-hoff foundation; Netherlands Organization for Health Research and DevelopmentNetherlands Organization for Health Research and Development [ZonMW-VIDI-917.76.329]; Utrecht University; We thank all members of the Ungermann group for discussion, J. Heinisch for antibodies, and Angela Perz and Nadine Decker (BZH) for technical support. This work was funded by the Deutsche Forschungsgemeinschaft (SFB431, CA806/2-1), the Fundacion Ramon Areces (to M. C.), and the Hans-Muhlen-hoff foundation (to C. U.). F. R. is supported by the Netherlands Organization for Health Research and Development (ZonMW-VIDI-917.76.329) and by the Utrecht University (High Potential grant). | |
dc.language.iso | en | |
dc.publisher | AMER SOC CELL BIOLOGY | |
dc.relation.ispartof | MOLECULAR BIOLOGY OF THE CELL | |
dc.subject | Cell Biology | |
dc.subject | DOCKING | |
dc.subject | GTPASE | |
dc.subject | KINASE | |
dc.subject | MEMBRANE | |
dc.subject | PROTEIN COMPLEX | |
dc.subject | PURIFICATION | |
dc.subject | TETHERING COMPLEX | |
dc.subject | TRANSPORT | |
dc.subject | VESICLE | |
dc.subject | YEAST SACCHAROMYCES-CEREVISIAE | |
dc.title | Vps41 Phosphorylation and the Rab Ypt7 Control the Targeting of the HOPS Complex to Endosome-Vacuole Fusion Sites | |
dc.type | journal article | |
dc.identifier.doi | 10.1091/mbc.E08-09-0943 | |
dc.identifier.isi | ISI:000264752100005 | |
dc.description.volume | 20 | |
dc.description.issue | 7 | |
dc.description.startpage | 1937 | |
dc.description.endpage | 1948 | |
dc.contributor.orcid | 0000-0002-2978-8255 | |
dc.contributor.orcid | 0000-0002-2978-8255 | |
dc.contributor.orcid | 0000-0003-2652-2686 | |
dc.contributor.orcid | 0000-0002-2677-6945 | |
dc.contributor.researcherid | F-3306-2016 | |
dc.contributor.researcherid | Y-1225-2019 | |
dc.contributor.researcherid | U-8327-2019 | |
dc.identifier.eissn | 19394586 | |
dc.publisher.place | 8120 WOODMONT AVE, STE 750, BETHESDA, MD 20814-2755 USA | |
dcterms.isPartOf.abbreviation | Mol. Biol. Cell | |
dcterms.oaStatus | Green Published | |
crisitem.author.netid | UnCh999 | - |
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geprüft am 28.05.2024