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Aquaporin Modulation by Cations, a Review.
Curr Issues Mol Biol, 46(8):7955-7975.
Aquaporins (AQPs) are transmembrane channels initially discovered for their rolein water flux facilitation through biological membranes. Over the years, a muchmore complex and subtle picture of these channels appeared, highlighting manyother solutes accommodated by AQPs and a dense regulatory network finely tuningcell membranes' water permeability. At the intersection between severaltransduction pathways (e.g., cell volume regulation, calcium signaling, potassiumcycling, etc.), this wide and ancient protein family is considered an importanttherapeutic target for cancer treatment and many other pathophysiologies.However, a precise and isoform-specific modulation of these channels function isstill challenging. Among the modulators of AQPs functions, cations have beenshown to play a significant contribution, starting with mercury beinghistorically associated with the inhibition of AQPs since their discovery. Whilethe comprehension of AQPs modulation by cations has improved, a unifyingmolecular mechanism integrating all current knowledge is still lacking. In aneffort to extract general trends, we reviewed all known modulations of AQPs bycations to capture a first glimpse of this regulatory network. We paid particularattention to the associated molecular mechanisms and pinpointed the residuesinvolved in cation binding and in conformational changes tied up to themodulation of the channel function.
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