Structure and Roles of V-type ATPases
| Autor: | Thamiya Vasanthakumar, John L. Rubinstein |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Gene isoform
Vacuolar Proton-Translocating ATPases Protein Conformation Protein subunit ATPase Saccharomyces cerevisiae Biochemistry 03 medical and health sciences 0302 clinical medicine Animals Humans V-ATPase Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences biology biology.organism_classification Cell biology Proton pump Enzyme chemistry biology.protein 030217 neurology & neurosurgery Function (biology) |
| Zdroj: | Trends in Biochemical Sciences. 45:295-307 |
| ISSN: | 0968-0004 |
| DOI: | 10.1016/j.tibs.2019.12.007 |
| Popis: | V-ATPases are membrane-embedded protein complexes that function as ATP hydrolysis-driven proton pumps. V-ATPases are the primary source of organellar acidification in all eukaryotes, making them essential for many fundamental cellular processes. Enzymatic activity can be modulated by regulated and reversible disassembly of the complex, and several subunits of mammalian V-ATPase have multiple isoforms that are differentially localized. Although the biochemical properties of the different isoforms are currently unknown, mutations in specific subunit isoforms have been associated with various diseases, making V-ATPases potential drug targets. V-ATPase structure and activity have been best characterized in Saccharomyces cerevisiae, where recent structures have revealed details about the dynamics of the enzyme, the proton translocation pathway, and conformational changes associated with regulated disassembly and autoinhibition. |
| Databáze: | OpenAIRE |
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