A universal mechanism for transport and regulation of CPA sodium proton exchangers

被引：16

作者：

Calinescu, Octavian ^{[1
,2
]}

Fendler, Klaus ^{[1
]}

机构：

[1] Max Planck Inst Biophys, Dept Biophys Chem, D-60438 Frankfurt, Germany

[2] Carol Davila Univ Med & Pharm, Fac Med, Dept Biophys, RO-050474 Bucharest, Romania

来源：

BIOLOGICAL CHEMISTRY | 2015年 / 396卷 / 9-10期

关键词：

cation/proton antiporter superfamily; Na+/H+ exchangers; NhaA; NhaP1; pH regulation; transport mechanism; NA+/H+ ANTIPORTER; CRYSTAL-STRUCTURE; PH REGULATION; MEMBRANE; NHAA; NA; MODEL;

D O I：

10.1515/hsz-2014-0278

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent studies performed on a series of Na+/H+ exchangers have led us to postulate a general mechanism for Na+/H+ exchange in the monovalent cation/proton antiporter superfamily. This simple mechanism employs a single binding site for which both substrates compete. The developed kinetic model is self-regulatory, ensuring down-regulation of transport activity at extreme pH, and elegantly explains the pH-dependent activity of Na+/H+ exchangers. The mechanism was experimentally verified and shown to describe both electrogenic and electroneutral exchangers. Using a small number of parameters, exchanger activity can be modeled under different conditions, providing insights into the physiological role of Na+/H+ exchangers.

引用

页码：1091 / 1096

页数：6

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