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  • Title: Structural basis for pH gating of plant aquaporins.
    Author: Frick A, Järvå M, Törnroth-Horsefield S.
    Journal: FEBS Lett; 2013 Apr 02; 587(7):989-93. PubMed ID: 23454640.
    Abstract:
    Plants have evolved to cope with fluctuations in water supply by gating their water channels known as aquaporins. During flooding, a rapid drop of cytosolic pH due to anoxia leads to a simultaneous closure of the aquaporins in the plasma membrane. The closing mechanism has been suggested to involve a conserved histidine on cytosolic loop D. Here we report the crystal structure of a spinach aquaporin at low pH, revealing for the first time the structural basis for how this pH-sensitive histidine helps to keep the aquaporin in a closed state.
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