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Antioxid Redox Signal. 2014 Feb 20;20(6):937-51. doi: 10.1089/ars.2013.5483. Epub 2013 Aug 20.

S-glutathionylation of ion channels: insights into the regulation of channel functions, thiol modification crosstalk, and mechanosensing.

Author information

1
1 Department of Neurology, Yale University School of Medicine , New Haven, Connecticut.

Abstract

SIGNIFICANCE:

Ion channels control membrane potential, cellular excitability, and Ca(++) signaling, all of which play essential roles in cellular functions. The regulation of ion channels enables cells to respond to changing environments, and post-translational modification (PTM) is one major regulation mechanism.

RECENT ADVANCES:

Many PTMs (e.g., S-glutathionylation, S-nitrosylation, S-palmitoylation, S-sulfhydration, etc.) targeting the thiol group of cysteine residues have emerged to be essential for ion channels regulation under physiological and pathological conditions.

CRITICAL ISSUES:

Under oxidative stress, S-glutathionylation could be a critical PTM that regulates many molecules. In this review, we discuss S-glutathionylation-mediated structural and functional changes of ion channels. Criteria for testing S-glutathionylation, methods and reagents used in ion channel S-glutathionylation studies, and thiol modification crosstalk, are also covered. Mechanotransduction, and S-glutathionylation of the mechanosensitive KATP channel, are discussed.

FUTURE DIRECTIONS:

Further investigation of the ion channel S-glutathionylation, especially the physiological significance of S-glutathionylation and thiol modification crosstalk, could lead to a better understanding of the thiol modifications in general and the ramifications of such modifications on cellular functions and related diseases.

PMID:
23834398
PMCID:
PMC3924852
DOI:
10.1089/ars.2013.5483
[Indexed for MEDLINE]
Free PMC Article

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