Structural insights into aquaporin selectivity and regulation

Abstract

Aquaporins have emerged as one of the structurally best-characterized membrane protein families, with fourteen different structures available from a diverse range of organisms. While all aquaporins share the same fold and passive mechanism for water permeation, structural details allow for differences in selectivity and modes of regulation. These details are now the emphasis of aquaporin structural biology. Recent structural studies of eukaryotic aquaporins have revealed reoccurring structural themes in both gating and trafficking, implying a limited number of structural solutions to aquaporin regulation. Moreover, the groundbreaking subangstrom resolution structure of a yeast aquaporin allows hydrogens to be visualized in the water-conducting channel, providing exclusive new insights into the proton exclusion mechanism.