Takeda Kozue, Cabrera Margarita, Rohde Jan, Bausch Dirk, Jensen Ole N, Ungermann Christian
Department of Biology, University of Osnabrück, Barbarastrasse 13, 49076 Osnabrück, Germany.
FEBS Lett. 2008 Apr 30;582(10):1558-63. doi: 10.1016/j.febslet.2008.03.055. Epub 2008 Apr 9.
At yeast vacuoles, phosphorylation of the HOPS subunit Vps41 depends on the Yck3 kinase. In a screen for mutants that mimic the yck3Delta phenotype, in which Vps41 accumulates in vacuolar dots, we observed that mutants in the V0-part of the V0/V1-ATPase, in particular in vma16Delta, also accumulate Vps41. This accumulation is not due to a phosphorylation defect, but to reduced release of Vps41 from vma16Delta vacuoles. One reason could be a connection to vacuole fission, which is blocked in V-ATPase mutants. Vacuole fusion is not impaired between vacuoles lacking the V0-subunits Vma16 or Vma6 and wild-type vacuoles, whereas fusion between mutant vacuoles is reduced. Our data suggest a connection between vacuole biogenesis and membrane fusion.
在酵母液泡中，HOPS亚基Vps41的磷酸化依赖于Yck3激酶。在筛选模拟yck3Δ表型（其中Vps41在液泡小点中积累）的突变体时，我们观察到V0/V1-ATP酶V0部分的突变体，特别是vma16Δ中的突变体，也会积累Vps41。这种积累不是由于磷酸化缺陷，而是由于Vps41从vma16Δ液泡中的释放减少。一个原因可能是与液泡分裂有关，而液泡分裂在V-ATP酶突变体中受阻。缺乏V0亚基Vma16或Vma6的液泡与野生型液泡之间的液泡融合没有受损，而突变体液泡之间的融合则减少。我们的数据表明液泡生物发生与膜融合之间存在联系。
