CLC channels and transporters: proteins with borderline personalities.

TitleCLC channels and transporters: proteins with borderline personalities.
Publication TypeJournal Article
Year of Publication2010
AuthorsAccardi A, Picollo A
JournalBiochim Biophys Acta
Date Published2010 Aug
KeywordsAnimals, Antiporters, Binding Sites, Chloride Channels, Chlorides, Humans, Ion Transport, Models, Anatomic, Nucleotides, Protein Structure, Tertiary, Protons

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.

Alternate JournalBiochim. Biophys. Acta
PubMed ID20188062
PubMed Central IDPMC2885512
Grant ListR01 GM085232-01A1 / GM / NIGMS NIH HHS / United States
R01 GM085232-04 / GM / NIGMS NIH HHS / United States