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Structure and function of aquaporin water channels
1Departments of Medicine and Physiology, Cardiovascular Research Institute, University of California, San Francisco 94143-0521, USA. verkman@itsa.ucsf.edu
American Journal of Physiology. Renal Physiology
|February 8, 2000
Summary
Aquaporins (AQPs) are membrane proteins crucial for fluid transport. This review details mammalian AQP structure, function, and potential as drug targets.
Area of Science:
- Biochemistry and Molecular Biology
- Cell Biology
- Structural Biology
Background:
- Aquaporins (AQPs) are small, membrane-spanning proteins essential for fluid transport across cell membranes.
- They assemble as homotetramers, with each monomer forming a distinct water pore.
Purpose of the Study:
- To review the molecular structure and function of mammalian aquaporins.
- To discuss recent findings on AQP roles and potential as drug targets.
Main Methods:
- Mutagenesis
- Epitope tagging
- Spectroscopic and freeze-fracture electron microscopy
- Electron cryocrystallography
Main Results:
- Mammalian AQPs exhibit diverse structures, forming water-selective pores or transporting larger solutes like glycerol.
- Evidence suggests possible ion and carbon dioxide transport, regulated by posttranslational modifications.
- Knockout mouse studies highlight multiple physiological roles for AQPs.
Conclusions:
- Mammalian aquaporins are vital for physiological processes, with varying selectivity for water and other solutes.
- Further research is needed to elucidate transport pathways and physiological significance.
- AQPs represent promising targets for structure-based drug discovery.