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Subunit structure, function, and arrangement in the yeast and coated vesicle V-ATPases
Takao Inoue1, Stephan Wilkens, Michael Forgac
1Department of Physiology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, Massachusetts 02111, USA.
Journal of Bioenergetics and Biomembranes
|November 26, 2003
Summary
Vacuolar (H+)-ATPases (V-ATPases) are proton pumps crucial for cellular acidification and transport. This review details their structure, function, and regulation, focusing on mammalian and yeast V-ATPases.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Vacuolar (H+)-ATPases (V-ATPases) are essential ATP-dependent proton pumps.
- They acidify intracellular compartments and transport protons across the plasma membrane.
- V-ATPases play roles in endocytosis, intracellular trafficking, protein processing, renal acidification, bone resorption, and pH homeostasis.
Purpose of the Study:
- To review research on V-ATPases from mammalian clathrin-coated vesicles and yeast.
- To elucidate the structure and subunit composition of V-ATPases.
- To investigate the mechanisms of V-ATPase function, regulation, and proton translocation.
Main Methods:
- Cysteine-mediated crosslinking
- Electron microscopy
- Site-directed and random mutagenesis
Main Results:
- Defined the overall shape and subunit locations within the V-ATPase and its V0 domain.
- Identified subunits and residues involved in ATP hydrolysis, proton translocation, and coupling.
- Investigated the mechanism of V-ATPase regulation via reversible dissociation.
Conclusions:
- V-ATPases are complex molecular machines with distinct V1 (hydrolysis) and V0 (transport) domains.
- Detailed structural and functional insights into V-ATPases have been gained through various biochemical and genetic techniques.
- Understanding V-ATPase regulation is key to comprehending their diverse cellular roles.