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2015 ; 593
(18
): 4129-38
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Structure and gating of CLC channels and exchangers
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Accardi A
J Physiol
2015[Sep]; 593
(18
): 4129-38
PMID26148215
show ga
Since their serendipitous discovery the CLC family of Cl(-) transporting proteins
has been a never ending source of surprises. From their double-barrelled
architecture to their complex structure and divergence as channels and
transporters, the CLCs never cease to amaze biophysicists, biochemists and
physiologists alike. These unusual functional properties allow the CLCs to fill
diverse physiological niches, regulating processes that range from muscle
contraction to acidification of intracellular organelles, nutrient accumulation
and survival of bacteria to environmental stresses. Over the last 15 years, the
availability of atomic-level information on the structure of the CLCs, coupled to
the discovery that the family is divided into passive channels and secondary
active transporters, has revolutionized our understanding of their function.
These breakthroughs led to the identification of the key structural elements
regulating gating, transport, selectivity and regulation by ligands.
Unexpectedly, many lines of evidence indicate that the CLC exchangers function
according to a non-conventional transport mechanism that defies the fundamental
tenets of the alternating-access paradigm for exchange transport, paving the way
for future unexpected insights into the principles underlying active transport
and channel gating.
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