The vacuolar-type H(+)-ATPase acidifies intracellular compartments and is essential for many processes, including cotransport, guard cell movement, development, and tolerance to environmental stress. We have identified at least 26 genes encoding subunits of the vacuolar-type H(+)-ATPase in the Arabidopsis thaliana genome, although inconsistent nomenclature of these genes is confusing. The pump consists of subunits A through H of the peripheral V(1) complex, and subunits a, c, c" and d of the V(o) membrane sector. Most V(1) subunits are encoded by a single gene, whereas V(o) subunits are encoded by multiple genes found in duplicated segments of the genome. We propose to name these genes VHA-x, where x represents the letter code for each subunit. Applying a consistent nomenclature will help us to understand how the expression, assembly and activity of this pump are integrated with plant growth, signaling, development and adaptation.
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http://dx.doi.org/10.1016/s1360-1385(02)02240-9 | DOI Listing |
Autophagy
January 2025
State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Biotechnology, Beijing, China.
Cell Commun Signal
December 2024
College of Basic Medical Science, Jinzhou Medical University, Jinzhou, Liaoning, China.
Vacuolar-type H+-ATPase (V-ATPase) is a crucial proton pump that plays an essential role in maintaining intracellular pH homeostasis and a variety of physiological processes. This review provides an in-depth exploration of the structural components, functional mechanisms, and regulatory modes of V-ATPase in cancer cells. Comprising two main domains, V and V, V-ATPase drives the proton pump through ATP hydrolysis, sustaining the pH balance within the cell and organelles.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
December 2024
Molecular Medicine Program, The Hospital for Sick Children, Toronto, ON M5G 0A4, Canada.
Vacuolar-type ATPases (V-ATPases) are membrane-embedded proton pumps that acidify intracellular compartments in almost all eukaryotic cells. Homologous with ATP synthases, these multisubunit enzymes consist of a soluble catalytic V subcomplex and a membrane-embedded proton-translocating V subcomplex. The V and V subcomplexes can undergo reversible dissociation to regulate proton pumping, with reassociation of V and V requiring the protein complex known as RAVE (regulator of the ATPase of vacuoles and endosomes).
View Article and Find Full Text PDFInt J Mol Sci
November 2024
Department of Forensic Medicine, School of Basic Medicine, Soochow University, Suzhou 215123, China.
Mutual interaction between doxorubicin (DOX) and cardiomyocytes is crucial for cardiotoxicity progression. Cardiomyocyte injury is an important pathological feature of DOX-induced cardiomyopathy, and its molecular pathogenesis is multifaceted. In addition to the direct toxic effects of DOX on cardiomyocytes, DOX-induced exosomes in the extracellular microenvironment also regulate the pathophysiological states of cardiomyocytes.
View Article and Find Full Text PDFJ Struct Biol
December 2024
Molecular Medicine Program, The Hospital for Sick Children, Toronto M5G 0A4, Canada; Department of Medical Biophysics, The University of Toronto, Toronto M5G 1L7, Canada; Department of Biochemistry, The University of Toronto, Toronto M5S 1A8, Canada. Electronic address:
Electron cryomicroscopy (cryo-EM) has recently allowed determination of near-atomic resolution structures of membrane proteins and protein complexes embedded in lipid vesicles. However, particle selection from electron micrographs of these vesicles can be challenging due to the strong signal contributed from the lipid bilayer. This challenge often requires iterative and laborious particle selection workflows to generate a dataset of high-quality particle images for subsequent analysis.
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