Two physically distinct pores in the dimeric ClC-0 chloride channel

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Item Type:	Article
Title:	Two physically distinct pores in the dimeric ClC-0 chloride channel
Creators Name:	Ludewig, U., Pusch, M. and Jentsch, T.J.
Abstract:	The Torpedo chloride channel ClC-0 is the prototype of a large family of chloride channels that have roles in transepithelial transport and in regulating electrical excitability and cell volume. ClC-0 opens in bursts with two identical conductance levels of approximately 8pS. Hyperpolarization slowly increases the probability of bursts ('slow gating'), and depolarization increases channel opening within bursts ('fast gating'). Replacing serine 123 by threonine changes rectification, ion selectivity and gating, but retains the typical bursting behaviour with two identical independent albeit reduced, conductance states (approximately 1.5 pS). Coexpression with wild-type ClC-0, either as covalently linked concatamers or as independent proteins, leads to bursting channels with two different pores. Our experiments strongly suggest that conductance, ion selectivity and 'fast' gating are determined only by the single subunit forming a single pore, independent from the attached pore; in contrast, 'slow' gating is a function of both subunits. Thus ClC-0 is a homodimer with two largely independent pores.
Keywords:	4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid, Amino Acid Sequence, Chloride Channels, Electrochemistry, Ion Channel Gating, Kinetics, Molecular Sequence Data, Mutation, Protein Conformation, Recombinant Proteins, Torpedo, Animals, Xenopus
Source:	Nature
ISSN:	0028-0836
Publisher:	Nature Publishing Group
Volume:	383
Number:	6598
Page Range:	340-343
Date:	26 September 1996
Official Publication:	https://doi.org/10.1038/383340a0
PubMed:	View item in PubMed

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