Altered Distribution of the Yeast Plasma Membrane H+-ATPase as a Feature of Vacuolar H+-ATPase Null Mutants

Perzov, Natalie; Nelson, Hannah; Nelson, Nathan

doi:10.1074/jbc.m007011200

Cited by 36 publications

(27 citation statements)

References 60 publications

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“…Additionally, the comparative proteomic analysis showed very clearly the under-expression of several enzymes belonging to the carbohydrate metabolism group in herbicide-treated cells (Braconi et al, 2009). Our data were, again, in accordance with works studying cellular responses to oxidative stress (Godon et al, 1998;Magherini et al, 2007;Perzov et al, 2000;Sales et al 2000;Weeks et al, 2006) and underlined the susceptibility of glycolysis to oxidative insults. A decrease in the activity of glycolytic enzymes is thought to be beneficial during exposure to oxidants (Costa et al, 2002;Shanmuganathan et al, 2004).…”

Section: Proteomics and Redox-proteomics 431 Comparative Proteomic supporting

confidence: 77%

Saccharomyces Cerevisiae as a Tool to Evaluate the Effects of Herbicides on Eukaryotic Life

Braconi¹,

Bernardini²,

Millucci³

et al. 2011

Herbicides and Environment

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Section: Proteomics and Redox-proteomics 431 Comparative Proteomic supporting

confidence: 77%

Saccharomyces Cerevisiae as a Tool to Evaluate the Effects of Herbicides on Eukaryotic Life

Braconi¹,

Bernardini²,

Millucci³

et al. 2011

Herbicides and Environment

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“…Bowman and Bowman (37) isolated mutants in Neurospora crassa that were resistant to the specific V-ATPase inhibitor concanamycin A and discovered that they contained mutations in Pma1p. Mislocalization of Pma1 from the plasma membrane to the endoplasmic reticulum (38) or the vacuole (39) in the vma mutants has been reported, but the physiological implications of the altered localization have not been clarified. To address a potential coordination of function between the V-ATPase and Pma1p, we examined pH homeostasis under varied extracellular conditions in two vma mutants, vma2⌬ and vma3⌬.…”

mentioning

confidence: 99%

Vacuolar and Plasma Membrane Proton Pumps Collaborate to Achieve Cytosolic pH Homeostasis in Yeast

Martínez-Muñoz¹,

Kane

2008

Journal of Biological Chemistry

238

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Vacuolar proton-translocating ATPases (V-ATPases) play a central role in organelle acidification in all eukaryotic cells. To address the role of the yeast V-ATPase in vacuolar and cytosolic pH homeostasis, ratiometric pH-sensitive fluorophores specific for the vacuole or cytosol were introduced into wild-type cells and vma mutants, which lack V-ATPase subunits. Transiently glucose-deprived wild-type cells respond to glucose addition with vacuolar acidification and cytosolic alkalinization, and subsequent addition of K ؉ ion increases the pH of both the vacuole and cytosol. In contrast, glucose addition results in an increase in vacuolar pH in both vma mutants and wild-type cells treated with the V-ATPase inhibitor concanamycin A. Cytosolic pH homeostasis is also significantly perturbed in the vma mutants. Even at extracellular pH 5, conditions optimal for their growth, cytosolic pH was much lower, and response to glucose was smaller in the mutants. In plasma membrane fractions from the vma mutants, activity of the plasma membrane proton pump, Pma1p, was 65-75% lower than in fractions from wildtype cells. Immunofluorescence microscopy confirmed decreased levels of plasma membrane Pma1p and increased Pma1p at the vacuole and other compartments in the mutants. Pma1p was not mislocalized in concanamycin-treated cells, but a significant reduction in cytosolic pH under all conditions was still observed. We propose that short-term, V-ATPase activity is essential for both vacuolar acidification in response to glucose metabolism and for efficient cytosolic pH homeostasis, and long-term, V-ATPases are important for stable localization of Pma1p at the plasma membrane.The importance of V-ATPases 3 for acidification of the vacuole/lysosomes, Golgi apparatus, and endosomes of eukaryotic cells is well established (1, 2). Multiple cellular processes, including secondary transport of ions and metabolites, maturation of iron transporters, endocytic and biosynthetic protein sorting, and zymogen activation depend on compartment acidification and have been linked to V-ATPase activity (1, 3). In some cells such as macrophages, V-ATPases play specialized roles that clearly include regulation of cytosolic pH (4, 5). However, although V-ATPases pump protons from the cytosol into organelles in all cells, they are not generally believed to play a major role in cytosolic pH regulation.The yeast Saccharomyces cerevisiae has emerged as a major model system for eukaryotic V-ATPases. One reason for this is that yeast mutants lacking all V-ATPase activity (vma mutants) are viable, but loss of V-ATPase activity in eukaryotes other than fungi is lethal (6 -9). Yeast vma mutants do exhibit a set of distinctive phenotypes, however, that includes the inability to grow at pH values lower than 3 or higher than 7 and sensitivity to high extracellular calcium concentrations (2). This Vma Ϫ phenotype suggests a perturbation of pH homeostasis in these cells that is not fully understood. It has been suggested that vma mutants survive at low extracellular p...

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“…Germ tube formation during hyphal development requires alkalinization of the cytoplasm (62). In S. cerevisiae, V-ATPase mutants display an abnormally acidified cytosol because they either lack the Pma1p proton efflux pump at the cell surface (35,63,64) or Pma1p is not fully active (60). Stv1p-containing V-ATPase complexes present in the vph1⌬/⌬ mutant may be sufficient for proper localization of Pma1p and normal cytosolic alkalinization during hyphal development.…”

Section: Discussionmentioning

confidence: 99%

Deletion of Vacuolar Proton-translocating ATPase Voa Isoforms Clarifies the Role of Vacuolar pH as a Determinant of Virulence-associated Traits in Candida albicans*

Raines¹,

Rane

Bernardo

et al. 2013

Journal of Biological Chemistry

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Background: V-ATPase regulates pH, and Candida albicans virulence is pH-dependent. Results: Deletion of V-ATPase V o a subunit Vph1p, but not Stv1p, alkalinizes vacuoles; several virulence-related traits remain unaffected. Conclusion: Vacuolar acidification is not essential for in vitro filamentation, biofilm formation, and macrophage killing in C. albicans. Significance: Stv1p in non-vacuolar organelles may play important roles in C. albicans infectivity, particularly if Vph1p is not functional.

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Altered Distribution of the Yeast Plasma Membrane H+-ATPase as a Feature of Vacuolar H+-ATPase Null Mutants

Cited by 36 publications

References 60 publications

Saccharomyces Cerevisiae as a Tool to Evaluate the Effects of Herbicides on Eukaryotic Life

Saccharomyces Cerevisiae as a Tool to Evaluate the Effects of Herbicides on Eukaryotic Life

Vacuolar and Plasma Membrane Proton Pumps Collaborate to Achieve Cytosolic pH Homeostasis in Yeast

Deletion of Vacuolar Proton-translocating ATPase Voa Isoforms Clarifies the Role of Vacuolar pH as a Determinant of Virulence-associated Traits in Candida albicans*

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