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CFTR: Effect of ICL2 and ICL4 amino acids in close spatial proximity on the current properties of the channel

Abstract : CFTR is the only ABC transporter functioning as a chloride (Cl−) channel.We studied molecular determinants, which might distinguish CFTR from standard ABC transporters, and focused on the interface formed by the intracellular loops from the membrane spanning domains. Methods: Residues from ICL2 and ICL4 in close proximity were targeted, and their involvement in the functioning of CFTR was studied by whole cell patch clamp recording. Results: We identified 2 pairs of amino acids, at the extremity of the bundle formed by the four intracellular loops, whose mutation i) decreases the Cl− current of CFTR (couple E267-K1060) or ii) increases it with a change of the electrophysiological signature (couple S263-V1056). Conclusions: These results highlight the critical role of these ICL residues in the assembly of the different domains and/or in the Cl− permeation pathway of CFTR.
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https://hal.archives-ouvertes.fr/hal-00907930
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Submitted on : Friday, November 22, 2013 - 9:55:32 AM
Last modification on : Monday, October 11, 2021 - 2:23:10 PM

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Arnaud Billet, Jean-Paul Mornon, Mathilde Jollivet, Pierre Lehn, Isabelle Callebaut, et al.. CFTR: Effect of ICL2 and ICL4 amino acids in close spatial proximity on the current properties of the channel. Journal of Cystic Fibrosis, Elsevier, 2013, 12, pp.737-745. ⟨10.1016/j.jcf.2013.02.002⟩. ⟨hal-00907930⟩

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