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

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Calinescu,  Octavian
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;
Department of Biophysics, Faculty of Medicine, ‘Carol Davila’ University of Medicine and Pharmacy, RO-050474 Bucharest, Romania;

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Fendler,  Klaus
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Calinescu, O., & Fendler, K. (2015). A universal mechanism for transport and regulation of CPA sodium proton exchangers. Biological Chemistry, 396(9-10), 1091-1096. doi:10.1515/hsz-2014-0278.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-4108-7
Abstract
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.