CLC channels and transporters: Proteins with borderline personalities |
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Authors: | Alessio Accardi Alessandra Picollo |
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Affiliation: | a Department of Molecular Physiology and Biophysics, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA b Department of Anesthesiology, Weill Cornell Medical College, New York, NY, USA c Department of Physiology and Biophysics, Weill Cornell Medical College, New York, NY, USA d Department of Biochemistry, Weill Cornell Medical College, New York, NY, USA |
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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 β-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. |
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Keywords: | Chloride Channel Transporter Structure |
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