Regulation of pannexin channels by post-translational modifications
| Autor: | Silvia Penuela, Jamie Simek, Roger J. Thompson |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Cell type
Glycosylation Biophysics Biology Pannexin Panx3 Panx2 Biochemistry Panx1 Connexins chemistry.chemical_compound Structural Biology Genetics Animals Humans Phosphorylation Receptor Molecular Biology Cellular localization Kinase Cell Biology Channel Cell biology chemistry Caspases Proteolysis Nitrogen Oxides Protein Processing Post-Translational Function (biology) Post-translational modifications Ionotropic effect |
| Zdroj: | FEBS Letters. 588:1411-1415 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2014.01.028 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text