Structure, function and biogenesis of the fungal proton pump Pma1.


Journal

Biochimica et biophysica acta. Molecular cell research
ISSN: 1879-2596
Titre abrégé: Biochim Biophys Acta Mol Cell Res
Pays: Netherlands
ID NLM: 101731731

Informations de publication

Date de publication:
01 2024
Historique:
received: 19 04 2023
revised: 19 08 2023
accepted: 18 09 2023
medline: 20 11 2023
pubmed: 24 9 2023
entrez: 23 9 2023
Statut: ppublish

Résumé

The fungal plasma membrane proton pump Pma1 is an integral plasma membrane protein of the P-type ATPase family. It is an essential enzyme responsible for maintaining a constant cytosolic pH and for energising the plasma membrane to secondary transport processes. Due to its importance for fungal survival and absence from animals, Pma1 is also a highly sought-after drug target. Until recently, its characterisation has been limited to functional, mutational and localisation studies, due to a lack of high-resolution structural information. The determination of three cryo-EM structures of Pma1 in its unique hexameric state offers a new level of understanding the molecular mechanisms underlying the protein's stability, regulated activity and druggability. In light of this context, this article aims to review what we currently know about the structure, function and biogenesis of fungal Pma1.

Identifiants

pubmed: 37741574
pii: S0167-4889(23)00173-8
doi: 10.1016/j.bbamcr.2023.119600
pii:
doi:

Substances chimiques

Proton Pumps 0
Proton-Translocating ATPases EC 3.6.3.14
Membrane Proteins 0

Types de publication

Journal Article Review Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

119600

Subventions

Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/V007653/1
Pays : United Kingdom

Informations de copyright

Copyright © 2023 The Authors. Published by Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Margaret R Young (MR)

Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.

Sabine Heit (S)

Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.

Maike Bublitz (M)

Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom. Electronic address: maike.bublitz@bioch.ox.ac.uk.

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Classifications MeSH