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The vacuolar V 1 /V 0 ‐ATPase is involved in the release of the HOPS subunit Vps41 from vacuoles, vacuole fragmentation and fusion
Author(s) -
Takeda Kozue,
Cabrera Margarita,
Rohde Jan,
Bausch Dirk,
Jensen Ole N.,
Ungermann Christian
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.03.055
Subject(s) - vacuole , v atpase , microbiology and biotechnology , lipid bilayer fusion , phosphorylation , mutant , biology , fragmentation (computing) , protein subunit , cytoplasm , biochemistry , membrane , gene , ecology
At yeast vacuoles, phosphorylation of the HOPS subunit Vps41 depends on the Yck3 kinase. In a screen for mutants that mimic the yck3 Δ phenotype, in which Vps41 accumulates in vacuolar dots, we observed that mutants in the V 0 ‐part of the V 0 /V 1 ‐ATPase, in particular in vma16 Δ, also accumulate Vps41. This accumulation is not due to a phosphorylation defect, but to reduced release of Vps41 from vma16 Δ 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 V 0 ‐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.