期刊
MOLECULAR BIOLOGY OF THE CELL
卷 20, 期 7, 页码 1937-1948出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E08-09-0943
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资金
- Deutsche Forschungsgemeinschaft [SFB431, CA806/2-1]
- Fundacion Ramon Areces
- Hans-Muhlen-hoff foundation
- Netherlands Organization for Health Research and Development [ZonMW-VIDI-917.76.329]
- Utrecht University
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.
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