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Regulation of pannexin channels by post‐translational modifications
Author(s) -
Penuela Silvia,
Simek Jamie,
Thompson Roger J.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.01.028
Subject(s) - pannexin , microbiology and biotechnology , kinase , chemistry , biology , function (biology) , receptor , biochemistry , intracellular , gap junction , connexin
The large‐pore channels formed by the pannexin family of proteins have been implicated in many physiological and pathophysiological functions, mainly through their ATP release function. However, a tight regulation of channel opening is necessary to modulate their function in vivo. Post‐translational modifications have been postulated as some of the regulating mechanisms for Panx1, while Panx2 and Panx3 have not been as well characterized. Positive regulators include caspase cleavage to open Panx1 channels in apoptotic cells, and activation by Src family kinases via ionotropic receptors in neurons and macrophages. S‐nitrosylation of cysteines has been shown to both inhibit and activate the Panx1 channel in different cell types. All three pannexins are N‐glycosylated but to different levels of modification. Their diverse glycosylation appears to regulate cellular localization, intermixing, and may restrict their ability to function as inter‐cellular channels. It is clear that our understanding of pannexin post‐translational modification and their role in channel function regulation is still in its infancy even a decade after their discovery.