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https://hdl.handle.net/2440/51484
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Type: | Journal article |
Title: | Functional study of cytoplasmic loops of human skeletal muscle chloride channel, hClC-1 |
Author: | Ma, L. Rychkov, G. Bretag, A. |
Citation: | The International Journal of Biochemistry and Cell Biology, 2009; 41(6):1402-1409 |
Publisher: | Pergamon-Elsevier Science Ltd |
Issue Date: | 2009 |
ISSN: | 1357-2725 1878-5875 |
Statement of Responsibility: | Linlin Ma, Grigori Y. Rychkov and Allan H. Bretag |
Abstract: | The membrane-resident domain of chloride channels and transporters of the CLC family is composed of 18 alpha-helices (designated A to R) connected sequentially by extracellular and intracellular loops, whose functional characteristics are generally unclear. To study the relevance of the intracellular loops linking helices D and E, F and G, H and I and J and K, alanine-exchange mutagenesis, split channel strategy, GST (glutathione transferase)-pull-down methods and whole-cell patch-clamp recordings were used. We investigated the possible roles of these loops in binding to the cytoplasmic, carboxyl tail (C-tail) of the protein, as well as their physiological roles in channel function. Although other interacting positions are conceivable, our results indicate that there is unlikely to be significant binding between the C-tail and any one of these individual cytoplasmic loops. Particular loops might, however, be essential for some channel characteristics. For example, alanine-exchange mutation of the loop linking helix D to E eliminated channel currents; of the loop linking helix H to I caused a significant shift of the open probability of fast gating (P(o)(f)), towards more positive voltages; and of the loop linking helix J to K locked the common gating of hClC-1 open. Therefore, the gating mechanisms of hClC-1 might not only involve the helices and the C-tail, but also involve some of the loops. |
Keywords: | Muscle, Skeletal Cells, Cultured Cytoplasm Humans Alanine Chloride Channels Blotting, Western Transfection Gene Expression Protein Structure, Tertiary Structure-Activity Relationship |
DOI: | 10.1016/j.biocel.2008.12.006 |
Description (link): | http://www.elsevier.com/wps/find/journaldescription.cws_home/395/description#description |
Published version: | http://dx.doi.org/10.1016/j.biocel.2008.12.006 |
Appears in Collections: | Aurora harvest Molecular and Biomedical Science publications |
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