Characterization of Schizosaccharomyces pombe mutants defective in vacuolar acidification and protein sorting

T. Iwaki, T. Goa, N. Tanaka, K. Takegawa

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

The vacuolar H+ -ATPases (V-ATPases) are ATP-dependent proton pumps responsible for acidification of intracellular compartments in eukaryotic cells. To investigate the functional roles of the V-ATPase in Schizosaccharomyces pombe, the gene vma1 encoding subunit A or vma3 encoding subunit c was disrupted. Both deletion mutants lost the capacity for vacuolar acidification in vivo, and showed sensitivity to neutral pH or high concentrations of divalent cations including Ca2+. The delivery of FM4-64 to the vacuolar membrane and accumulation of Lucifer Yellow CH were strongly inhibited in the vma1 and vma3 mutants. Moreover, deletion of the S. pombe vma1 or vma3+ gene resulted in pleiotropic phenotypes consistent with lack of vacuolar acidification, including the missorting of vacuolar carboxypeptidase Y, abnormal vacuole morphology, and mating defects. These findings suggest that V-ATPase is essential for endocytosis, ion and pH homeostasis, and for intracellular targeting of vacuolar proteins and vacuolar biogenesis in S. pombe.

Original languageEnglish
Pages (from-to)197-207
Number of pages11
JournalMolecular Genetics and Genomics
Volume271
Issue number2
DOIs
Publication statusPublished - Mar 1 2004
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

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