首页> 外文期刊>FEBS letters. >The vacuolar V1/V0-ATPase is involved in the release of the HOPS subunit Vps41 from vacuoles, vacuole fragmentation and fusion.
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The vacuolar V1/V0-ATPase is involved in the release of the HOPS subunit Vps41 from vacuoles, vacuole fragmentation and fusion.

机译:液泡V1 / V0-ATP酶参与从液泡释放HOPS亚基Vps41,液泡片段化和融合。

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摘要

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.
机译:在酵母液泡中,HOPS亚基Vps41的磷酸化取决于Yck3激酶。在筛选模仿yck3Delta表型的突变体(其中Vps41在液泡点中积累)的筛选中,我们观察到V0 / V1-ATPase V0部分(尤其是vma16Delta)中的突变体也积累了Vps41。这种积累不是由于磷酸化缺陷,而是由于从vma16Delta液泡释放的Vps41减少。原因之一可能与液泡裂变有关,而液泡裂变在V-ATPase突变体中受阻。在缺少V0亚基Vma16或Vma6的液泡与野生型液泡之间,液泡融合不会受到损害,而突变液泡之间的融合却减少了。我们的数据表明液泡生物发生与膜融合之间的联系。

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