Calmodulin Gates Aquaporin 0 Permeability through a Positively Charged Cytoplasmic Loop.

ABSTRACT: Aquaporin 0 (AQP0), the major intrinsic protein of the eye lens, plays a vital role in maintaining lens clarity by facilitating the transport of water across lens fiber cell membranes. AQP0 reduces its osmotic water permeability constant (P_f) in response to increases in the external calcium concentration, an effect that is mediated by an interaction with the calcium-binding messenger protein, calmodulin (CaM), and phosphorylation of the CaM-binding site abolishes calcium sensitivity. Despite recent structural characterization of the AQP0-CaM complex, the mechanism by which CaM modulates AQP0 remains poorly understood. By combining atomistic molecular dynamics simulations and oocyte permeability assays, we conclude that serine phosphorylation of AQP0 does not inhibit CaM binding

SUBMITTER: Fields JB 

PROVIDER: S-EPMC5217678 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature