Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
Biophys J
2005 Jun 01;886:3936-45. doi: 10.1529/biophysj.104.055012.
Show Gene links
Show Anatomy links
Oxidation and reduction control of the inactivation gating of Torpedo ClC-0 chloride channels.
Li Y, Yu WP, Lin CW, Chen TY.
???displayArticle.abstract???
Oxidation and reduction (redox) are known to modulate the function of a variety of ion channels. Here, we report a redox regulation of the function of ClC-0, a chloride (Cl(-)) channel from the Torpedo electric organ. The study was motivated by the occasional observation of oocytes with hyperpolarization-activated Cl(-) current when these oocytes expressed ClC-0. We find that these atypical recording traces can be turned into typical ClC-0 current by incubating the oocyte in millimolar concentrations of reducing agents, suggesting that the channel function is regulated by oxidation and reduction. The redox control apparently results from an effect of oxidation on the slow (inactivation) gating: oxidation renders it more difficult for the channel to recover from the inactivated states. Introducing the point mutation C212S in ClC-0 suppresses the inactivation state, and this inactivation-suppressed mutant is no longer sensitive to the inhibition by oxidizing reagents. However, C212 is probably not the target for the redox reaction because the regulation of the inactivation gating by oxidation is still present in a pore mutant (K165C/K165 heterodimer) in which the C212S mutation is present. Taking advantage of the K165C/K165 heterodimer, we further explore the oxidation effect in ClC-0 by methane thiosulfonate (MTS) modifications. We found that trimethylethylammonium MTS modification of the introduced cysteine can induce current in the K165C/K165 heterodimer, an effect attributed to the recovery of the channel from the inactivation state. The current induction by MTS reagents is subjected to redox controls, and thus the extent of this current induction can serve as an indicator to report the oxidation state of the channel. These results together suggest that the inactivation gating of ClC-0 is affected by redox regulation. The finding also provides a convenient method to "cure" those atypical recording traces of ClC-0 expressed in Xenopus oocytes.
Accardi,
Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels.
2004, Pubmed
Accardi,
Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels.
2004,
Pubmed Accardi,
Ionic currents mediated by a prokaryotic homologue of CLC Cl- channels.
2004,
Pubmed Bauer,
Completely functional double-barreled chloride channel expressed from a single Torpedo cDNA.
1991,
Pubmed
,
Xenbase Chen,
Side-chain charge effects and conductance determinants in the pore of ClC-0 chloride channels.
2003,
Pubmed Chen,
Extracellular zinc ion inhibits ClC-0 chloride channels by facilitating slow gating.
1998,
Pubmed
,
Xenbase Chen,
Different fast-gate regulation by external Cl(-) and H(+) of the muscle-type ClC chloride channels.
2001,
Pubmed
,
Xenbase Chen,
Nonequilibrium gating and voltage dependence of the ClC-0 Cl- channel.
1996,
Pubmed Claiborne,
Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation.
1999,
Pubmed Doyle,
The structure of the potassium channel: molecular basis of K+ conduction and selectivity.
1998,
Pubmed Dutzler,
X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity.
2002,
Pubmed Dutzler,
Gating the selectivity filter in ClC chloride channels.
2003,
Pubmed
,
Xenbase Fahlke,
Pore stoichiometry of a voltage-gated chloride channel.
1998,
Pubmed Feng,
Transmembrane redox sensor of ryanodine receptor complex.
2000,
Pubmed Gross,
Agitoxin footprinting the shaker potassium channel pore.
1996,
Pubmed
,
Xenbase Hanke,
Single chloride channels from Torpedo electroplax. Activation by protons.
1983,
Pubmed Iyer,
A biological role for prokaryotic ClC chloride channels.
2002,
Pubmed Jentsch,
Molecular structure and physiological function of chloride channels.
2002,
Pubmed Jentsch,
The CLC chloride channel family.
1999,
Pubmed Lin,
Elimination of the slow gating of ClC-0 chloride channel by a point mutation.
1999,
Pubmed
,
Xenbase Lin,
Probing the pore of ClC-0 by substituted cysteine accessibility method using methane thiosulfonate reagents.
2003,
Pubmed Lin,
Cysteine modification of a putative pore residue in ClC-0: implication for the pore stoichiometry of ClC chloride channels.
2000,
Pubmed
,
Xenbase Liu,
Dynamic rearrangement of the outer mouth of a K+ channel during gating.
1996,
Pubmed Ludewig,
Two physically distinct pores in the dimeric ClC-0 chloride channel.
1996,
Pubmed
,
Xenbase Maduke,
A decade of CLC chloride channels: structure, mechanism, and many unsettled questions.
2000,
Pubmed Maduke,
Formation of CLC-0 chloride channels from separated transmembrane and cytoplasmic domains.
1998,
Pubmed
,
Xenbase Middleton,
Homodimeric architecture of a ClC-type chloride ion channel.
1996,
Pubmed Miller,
Open-state substructure of single chloride channels from Torpedo electroplax.
1982,
Pubmed Miller,
Dimeric structure of single chloride channels from Torpedo electroplax.
1984,
Pubmed Pessah,
Functional role of hyperreactive sulfhydryl moieties within the ryanodine receptor complex.
2000,
Pubmed Pusch,
Gating of the voltage-dependent chloride channel CIC-0 by the permeant anion.
1995,
Pubmed
,
Xenbase Pusch,
Temperature dependence of fast and slow gating relaxations of ClC-0 chloride channels.
1997,
Pubmed
,
Xenbase Saviane,
The muscle chloride channel ClC-1 has a double-barreled appearance that is differentially affected in dominant and recessive myotonia.
1999,
Pubmed
,
Xenbase Tang,
Oxidative regulation of large conductance calcium-activated potassium channels.
2001,
Pubmed van Montfort,
Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B.
2003,
Pubmed Wang,
Catalytic inactivation of protein tyrosine phosphatase CD45 and protein tyrosine phosphatase 1B by polyaromatic quinones.
2004,
Pubmed Xia,
Skeletal muscle ryanodine receptor is a redox sensor with a well defined redox potential that is sensitive to channel modulators.
2000,
Pubmed Zeidner,
Redox-dependent gating of G protein-coupled inwardly rectifying K+ channels.
2001,
Pubmed
,
Xenbase
