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Pores Formed by Single Subunits in Mixed Dimers of Different CLC Chloride Channels

Weinreich, Frank, Jentsch, Thomas J.·2001·Journal of Biological Chemistry
DOI 10.1074/jbc.m005733200
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Abstract

CLC chloride channels comprise a gene family with nine mammalian members. Probably all CLC channels form homodimers, and some CLC proteins may also associate to heterodimers. ClC-0 and ClC-1, the only CLC channels investigated at the single-channel level, display two conductances of equal size which are thought to result from two separate pores, formed individually by the two monomers. We generated concatemeric channels containing one subunit of ClC-0 together with one subunit of ClC-1 or ClC-2. They should display two different conductances if one monomer were sufficient to form one pore. Indeed, we found a 8-picosiemens (pS) conductance (corresponding to ClC-0) that was associated with either a 1.8-pS (ClC-1) or a 2.8-pS (ClC-2) conductance. These conductances retained their typical gating, but the slow gating of ClC-0 that affects both pores simultaneously was lost. ClC-2 and ClC-0 current components were modified by point mutations in the corresponding subunit. The ClC-2 single pore of the mixed dimer was compared with the pores in the ClC-2 homodimer and found to be unaltered. We conclude that each monomer individually forms a gated pore. CLC dimers in general must be imagined as having two pores, as shown previously for ClC-0.

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  • The two pathways are not segregated to each subunit as in CLC channels; instead each pore comprises side chains from TM2, TM3b, and TM4 of one subunit plus the TM3-break phenylalanine from the opposing subunit.

    “The two pathways are not segregated to each subunit as in CLC channels24; instead each pore comprises side chains from TM2, TM3b, and TM4 of one subunit plus the TM3-break phenylalanine from the opposing subunit.”

    From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [24]

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Metadata

Authors
Weinreich, F., & Jentsch, T. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2001-01
Volume
276
Issue
4
Pages
2347-2353
ISSN
0021-9258
DOI
10.1074/jbc.m005733200
Cited by
131
References
0
Language
en
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