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Biochim Biophys Acta. 2010 Aug;1798(8):1457-64. doi: 10.1016/j.bbamem.2010.02.022. Epub 2010 Feb 24.

CLC channels and transporters: proteins with borderline personalities.

Author information

1
Department of Molecular Physiology and Biophysics, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA. ala2022@med.cornell.edu

Abstract

Controlled chloride movement across membranes is essential for a variety of physiological processes ranging from salt homeostasis in the kidneys to acidification of cellular compartments. The CLC family is formed by two, not so distinct, sub-classes of membrane transport proteins: Cl(-) channels and H(+)/Cl(-) exchangers. All CLC's are homodimers with each monomer forming an individual Cl- permeation pathway which appears to be largely unaltered in the two CLC sub-classes. Key residues for ion binding and selectivity are also highly conserved. Most CLC's have large cytosolic carboxy-terminal domains containing two cystathionine beta-synthetase (CBS) domains. The C-termini are critical regulators of protein trafficking and directly modulate Cl- by binding intracellular ATP, H+ or oxidizing compounds. This review focuses on the recent mechanistic insights on the how the structural similarities between CLC channels and transporters translate in unexpected mechanistic analogies between these two sub-classes.

PMID:
20188062
PMCID:
PMC2885512
DOI:
10.1016/j.bbamem.2010.02.022
[Indexed for MEDLINE]
Free PMC Article

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