Regulation of V-ATPase activity
| Autor: | Christina McGuire, Kristina Cotter, Michael Forgac, Laura A. Stransky |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
Mammals
Models Molecular 0301 basic medicine Vacuolar Proton-Translocating ATPases Cell signaling Saccharomyces cerevisiae Proteins Chemistry Protein subunit Growth factor medicine.medical_treatment Cellular differentiation Cell biology Protein Subunits Protein Transport 03 medical and health sciences 030104 developmental biology medicine Animals Humans Insect Proteins V-ATPase Secretion Protein Multimerization Cellular compartment Intracellular |
| Zdroj: | Frontiers in Bioscience. 22:609-622 |
| ISSN: | 1093-4715 1093-9946 |
| DOI: | 10.2741/4506 |
| Popis: | V-ATPases are ATP-driven proton pumps present in both intracellular and cell surface membranes of eukaryotes that function in many normal and disease processes. V-ATPases are large, multi-subunit complexes composed of a peripheral domain (V1) that hydrolyzes ATP and a membrane integral domain (V0) that translocates protons. Because of the diversity of their functions, V-ATPase activity is controlled by a number of mechanisms. Regulated assembly of the V1 and V0 domains rapidly modulates V-ATPase activity in response to a variety of cues, including nutrient availability, growth factor stimulation and cellular differentiation. Considerable information has recently emerged concerning the cellular signaling pathways controlling regulated assembly. Acid secretion by epithelial cells in the kidney and epididymus is controlled by regulated trafficking of V-ATPases to the cell surface. Isoforms of subunit a of the V0 domain both control trafficking of V-ATPases to distinct cellular membranes and confer properties to the resultant complexes that help account for differences in pH between cellular compartments. Finally, differential expression of genes encoding V-ATPases subunits occurs in a number of contexts, including cancer. |
| Databáze: | OpenAIRE |
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