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Interactions of Pannexin1 channels with purinergic and NMDA receptor channels
Pannexins are a three-member family of vertebrate plasma membrane spanning molecules that have homology to the invertebrate gap junction forming proteins, the innexins. However, pannexins do not form gap junctions but operate as plasma membrane channels. The best-characterized member of these protei...
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Published in: | Biochimica et biophysica acta 2018-01, Vol.1860 (1), p.166-173 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Pannexins are a three-member family of vertebrate plasma membrane spanning molecules that have homology to the invertebrate gap junction forming proteins, the innexins. However, pannexins do not form gap junctions but operate as plasma membrane channels. The best-characterized member of these proteins, Pannexin1 (Panx1) was suggested to be functionally associated with purinergic P2X and N-methyl-D-aspartate (NMDA) receptor channels. Activation of these receptor channels by their endogenous ligands leads to cross-activation of Panx1 channels. This in turn potentiates P2X and NMDA receptor channel signaling. Two potentiation concepts have been suggested: enhancement of the current responses and/or sustained receptor channel activation by ATP released through Panx1 pore and adenosine generated by ectonucleotidase-dependent dephosphorylation of ATP. Here we summarize the current knowledge and hypotheses about interactions of Panx1 channels with P2X and NMDA receptor channels. This article is part of a Special Issue entitled: Gap Junction Proteins edited by Jean Claude Herve.
•The hexameric protein Pannexin1 operates as a plasma membrane channel.•Activated P2X and N-methyl-D-aspartate receptors cross activate Pannexin1 channels.•Turn on Pannexin1 potentiates P2X and N-methyl-D-aspartate receptor signaling. |
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ISSN: | 0005-2736 0006-3002 1879-2642 1878-2434 |
DOI: | 10.1016/j.bbamem.2017.03.025 |