Proton transport and pH control in fungi
Open accessAbstract
Despite diverse and changing extracellular environments, fungi maintain a relatively constant cytosolic pH and numerous organelles of distinct lumenal pH. Key players in fungal pH control are V-ATPases and the P-type proton pump Pma1. These two proton pumps act in concert with a large array of other transporters and are highly regulated. The activities of Pma1 and the V-ATPaseare coordinated under some conditions, suggesting that pH in the cytosol and organelles is not controlled independently. Genomic studies, particularly in the highly tractable S. cerevisiae, are beginning to provide a systems-level view of pH control, including transcriptional responses to acid or alkaline ambient pH and definition of the full set of regulators required to maintain pH homeostasis. Genetically encoded pH sensors have provided new insights into localized mechanisms of pH control, as well as highlighting the dynamic nature of pH responses to the extracellular environment. Recent studies indicate that cellular pH plays a genuine signaling role that connects nutrient availability and growth rate through a number of mechanisms. Many of the pH control mechanisms found in S. cerevisiae are shared with other fungi, with adaptations for their individual physiological contexts. Fungi deploy certain proton transport and pH control mechanisms not shared with other eukaryotes; these regulators of cellular pH are potential antifungal targets. This re view describes current and emerging knowledge proton transport and pH control mechanisms in S. cerevisiae and briefly discusses how these mechanisms vary among fungi.
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Pma1 is a fungal plasma-membrane single-subunit P-type H+-ATPase that extrudes protons across the plasma membrane at the expense of ATP hydrolysis, contributing to cytosolic pH regulation and generation of the transmembrane electrochemical proton gradient that drives secondary nutrient transport.
“Pma1, encoded by PMA1, is a fungal plasma-membrane single-subunit P-type H+-ATPase that extrudes protons across the plasma membrane at the expense of ATP hydrolysis, thereby contributing to cytosolic pH regulation and to the generation of the transmembrane electrochemical proton gradient that drives secondary nutrient transport [32,33,34].”
From Ovotransferrin and Its γ-Core-Containing Peptides Impair Pma1-Dependent Proton Homeostasis in Candida albicans (2026) · cites this paper as [34]
Section 3.1 identifies Pma1 as a single-subunit plasma-membrane P-type H+-ATPase and describes its ATP consumption, electrogenic H+ transport, and role in cytosolic pH and membrane potential. The passages found do not establish the further claim that its proton gradient drives secondary nutrient transport; no page numbers were available in our copy. (LLM, conf=0.83)
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Research works printed but not linked: 2
- [97]Diakov TT Kane PM 2010 Regulation of V-ATPase activity and assembly by extracellular pH J Biol Chem M110.110122 [pii] 10.1074/jbc.M110.110122 PMC2911326 20511227 · DOI
- [114]Hirata R Takatsuki A 2001 Role of organelle acidification in intracellular protein transport RIKEN Review 41 90 91
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Santos-Pereira, C., Andrés, M. T., Chaves, S. R., Fierro, J. F., Gerós, H., Manon, S., Rodrigues, L. R., & Côrte-Real, M. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.12.224 · Cited by 21 · see citing works
Antuña, V., Fierro, P., Fierro, J. F., Álvarez, Á. L., & Andrés, M. T. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27167415
“It uses ATP to extrude protons and thereby helps maintain cytosolic pH, membrane potential, and the proton gradient required for secondary transport [32–34].”
- Authors
- Kane, P. M.
- Affiliations
- SUNY Upstate Medical University (US)
- Corresponding author
- Kane, Patricia M.
- ORCID
- Kane, Patricia M.
- Venue
- Advances in Experimental Medicine and Biology
- Publisher
- Springer International Publishing
- Published
- 2016
- Volume
- 892
- Pages
- 33-68
- ISSN
- 0065-2598 (ISSN-L)
- 2214-8019
- PMC
- PMC5957285
- OpenAlex
- W2345147274
- Semantic Scholar
- a981d86a6d129011e242938382935e1dcb2cbbfb
- Cited by
- 131
- References
- 192
- Citations by year
- 2026: 13 · 2025: 11 · 2024: 17 · 2023: 18 · 2022: 15 · 2021: 12 · 2020: 19 · 2019: 9 · 2018: 10 · 2017: 5 · 2016: 2
- FWCI
- 9.03
- Type
- book chapter
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Advances in experimental medicine and biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R01-GM50322, R01GM050322)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- proton transport, pH homeostasis, fungi, V-ATPase, Pma1, intracellular pH, Saccharomyces cerevisiae, pH sensor, pH signaling, antifungal drug targets, proton transporters
- MeSH terms
- Cell Membrane, Proton-Translocating ATPases, Hydrogen-Ion Concentration, Models, Molecular, Protons, Saccharomyces cerevisiae, Species Specificity, Vacuoles, Signal Transduction, Gene Expression, Ion Transport, Vacuolar Proton-Translocating ATPases, Saccharomyces cerevisiae Proteins
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