Reference - PMID:14735354 - Characterization of Schizosaccharomyces pombe mutants defective in vacuolar acidification and protein sorting.
Reference summary
- PubMed ID
- PMID:14735354
- Title
- Characterization of Schizosaccharomyces pombe mutants defective in vacuolar acidification and protein sorting.
- Authors
- Iwaki T, Goa T, Tanaka N, Takegawa K
- Citation
- Mol Genet Genomics 2004 Mar;271(2):197-207
- Publication year
- 2004
- 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.
