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CLC channels and transporters: proteins with borderline personalities Accardi A; Picollo ABiochim Biophys Acta 2010[Aug]; 1798 (8): 1457-64Controlled 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.|Animals[MESH]|Antiporters/chemistry/metabolism[MESH]|Binding Sites[MESH]|Chloride Channels/chemistry/*metabolism[MESH]|Chlorides/metabolism[MESH]|Humans[MESH]|Ion Transport[MESH]|Models, Anatomic[MESH]|Nucleotides/metabolism[MESH]|Protein Structure, Tertiary[MESH]|Protons[MESH] |
