Movement of hClC-1 C-termini during common gating and limits on their cytoplasmic location

Ma, Linlin, Rychkov, Grigori Y., Bykova, Ekaterina A., Zheng, Jie and Bretag, Allan H. (2011) Movement of hClC-1 C-termini during common gating and limits on their cytoplasmic location. Biochemical Journal, 436 436: 415-428. doi:10.1042/BJ20102153

Author Ma, Linlin
Rychkov, Grigori Y.
Bykova, Ekaterina A.
Zheng, Jie
Bretag, Allan H.
Title Movement of hClC-1 C-termini during common gating and limits on their cytoplasmic location
Journal name Biochemical Journal   Check publisher's open access policy
ISSN 0264-6021
Publication date 2011-03-17
Sub-type Article (original research)
DOI 10.1042/BJ20102153
Volume 436
Issue 436
Start page 415
End page 428
Total pages 14
Place of publication London,United Kingdom
Publisher Portland Press
Collection year 2012
Language eng
Formatted abstract
Functionally, the dimeric human skeletal muscle chloride channel hClC-1 is characterized by two distinctive gating processes, fast (protopore) gating and slow (common) gating. Of these, common gating is poorly understood, but extensive conformational rearrangement is suspected. To examine this possibility, we used FRET (fluorescence resonance energy transfer) and assessed the effects of manipulating the common-gating process. Closure of the common gate was accompanied by a separation of the Ctermini, whereas, with opening, the C-termini approached each other more closely. These movements were considerably smaller than those seen in ClC-0. To estimate the C-terminus depth within the cytoplasm we constructed a pair of split hClC-1 fragments tagged extracellularly and intracellularly respectively. These not only combined appropriately to rescue channel function, but we detected positive FRET between them. This restricts the C-termini of hClC-1 to a position close to its membrane-resident domain. From mutants in which fast or common gating were affected, FRET revealed a close linkage between the two gating processes with the carboxyl group of Glu232 apparently acting as the final effector for both. 
Keyword C-terminus
Common gating
Conformation change
Cytoplasmic domain
Human skeletal muscle chloride channel (hClC-1)
Fluorescence resonance energy transfer (FRET)
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
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Created: Tue, 07 Feb 2012, 11:54:27 EST by Susan Allen on behalf of Institute for Molecular Bioscience