Structural basis for pH gating of plant aquaporins.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Frick A,Järvå M,Törnroth-Horsefield S

doi

10.1016/j.febslet.2013.02.038

subject

Has Abstract

pub_date

2013-04-02 00:00:00

pages

989-93

issue

7

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(13)00184-1

journal_volume

587

pub_type

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