Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2049132 | FEBS Letters | 2008 | 6 Pages |
Abstract
At yeast vacuoles, phosphorylation of the HOPS subunit Vps41 depends on the Yck3 kinase. In a screen for mutants that mimic the yck3Δ phenotype, in which Vps41 accumulates in vacuolar dots, we observed that mutants in the V0-part of the V0/V1-ATPase, in particular in vma16Δ, also accumulate Vps41. This accumulation is not due to a phosphorylation defect, but to reduced release of Vps41 from vma16Δ 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.
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Authors
Kozue Takeda, Margarita Cabrera, Jan Rohde, Dirk Bausch, Ole N. Jensen, Christian Ungermann,