Abstract
Aquaporins (AQPs ) are a family of membrane water channels that basically function as regulators of intracellular and intercellular water flow. To date, thirteen AQPs , which are distributed widely in specific cell types in various organs and tissues, have been characterized in humans. Four AQP monomers, each of which consists of six membrane-spanning alpha-helices that have a central water-transporting pore, assemble to form tetramers, forming the functional units in the membrane. AQP facilitates osmotic water transport across plasma membranes and thus transcellular fluid movement. The cellular functions of aquaporins are regulated by posttranslational modifications , e.g. phosphorylation, ubiquitination, glycosylation, subcellular distribution, degradation, and protein interactions. Insight into the molecular mechanisms responsible for regulated aquaporin trafficking and synthesis is proving to be fundamental for development of novel therapeutic targets or reliable diagnostic and prognostic biomarkers.
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