Zinc Modulation of Water Permeability Reveals That Aquaporin 0 Functions As a Cooperative Tetramer

Overview

Journal J Gen Physiol

Specialty Physiology

Date 2007 Oct 17

PMID 17938229

Citations 18

Authors

Karin L Nemeth-Cahalan

Katalin Kalman

Alexandrine Froger

James E Hall

Affiliations

Soon will be listed here.

Abstract

We previously showed that the water permeability of AQP0, the water channel of the lens, increases with acid pH and that His40 is required (Németh-Cahalan, K.L., and J.E. Hall. 2000. J. Biol. Chem. 275:6777-6782; Németh-Cahalan, K.L., K. Kalman, and J.E. Hall. 2004. J. Gen. Physiol. 123:573-580). We have now investigated the effect of zinc (and other transition metals) on the water permeability of AQP0 expressed in Xenopus oocytes and determined the amino acid residues that facilitate zinc modulation. Zinc (1 mM) increased AQP0 water permeability by a factor of two and prevented any additional increase induced by acid pH. Zinc had no effect on water permeability of AQP1, AQP4 or MIPfun (AQP0 from killifish), or on mutants of AQP1 and MIPfun with added external histidines. Nickel, but not copper, had the same effect on AQP0 water permeability as zinc. A fit of the concentration dependence of the zinc effect to the Hill equation gives a coefficient greater than three, suggesting that binding of more than one zinc ion is necessary to enhance water permeability. His40 and His122 are necessary for zinc modulation of AQP0 water permeability, implying structural constraints for zinc binding and functional modulation. The change in water permeability was highly sensitive to a coinjected zinc-insensitive mutant and a single insensitive monomer completely abolished zinc modulation. Our results suggest a model in which positive cooperativity among subunits of the AQP0 tetramer is required for zinc modulation, implying that the tetramer is the functional unit. The results also offer the possibility of a pharmacological approach to manipulate the water permeability and transparency of the lens.

Citing Articles

Zebrafish Optical Development Requires Regulated Water Permeability by Aquaporin 0.

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Aquaporin Modulation by Cations, a Review.

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Deciphering Molecular Mechanisms Involved in the Modulation of Human Aquaporins' Water Permeability by Zinc Cations: A Molecular Dynamics Approach.

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In vivo macromolecular crowding is differentially modulated by aquaporin 0 in zebrafish lens: Insights from a nanoenvironment sensor and spectral imaging.

Vorontsova I, Vallmitjana A, Torrado B, Schilling T, Hall J, Gratton E Sci Adv. 2022; 8(7):eabj4833.

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Nutritional and Physiological Regulation of Water Transport in the Conceptus.

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