Department of Anesthesiology

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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
Volume1798
Issue8
Pagination1457-64
Date Published2010 Aug
ISSN0006-3002
KeywordsAnimals, Antiporters, Binding Sites, Chloride Channels, Chlorides, Humans, Ion Transport, Models, Anatomic, Nucleotides, Protein Structure, Tertiary, Protons
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.

DOI10.1016/j.bbamem.2010.02.022
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