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Pannexin-1 as a potentiator of ligand-gated receptor signaling
Pannexins are a class of plasma membrane spanning proteins that presumably form a hexameric, non-selective ion channel. Although similar in secondary structure to the connexins, pannexins notably do not form endogenous gap junctions and act as bona fide ion channels. The pannexins have been primaril...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4048300/ https://www.ncbi.nlm.nih.gov/pubmed/24576994 http://dx.doi.org/10.4161/chan.27978 |
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author | Isakson, Brant E Thompson, Roger J |
author_facet | Isakson, Brant E Thompson, Roger J |
author_sort | Isakson, Brant E |
collection | PubMed |
description | Pannexins are a class of plasma membrane spanning proteins that presumably form a hexameric, non-selective ion channel. Although similar in secondary structure to the connexins, pannexins notably do not form endogenous gap junctions and act as bona fide ion channels. The pannexins have been primarily studied as ATP-release channels, but the overall diversity of their functions is still being elucidated. There is an intriguing theme with pannexins that has begun to develop. In this review we analyze several recent reports that converge on the idea that pannexin channels (namely Panx1) can potentiate ligand-gated receptor signaling. Although the literature remains sparse, this emerging concept appears consistent between both ionotropic and metabotropic receptors of several ligand families. |
format | Online Article Text |
id | pubmed-4048300 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-40483002015-03-01 Pannexin-1 as a potentiator of ligand-gated receptor signaling Isakson, Brant E Thompson, Roger J Channels (Austin) Review Pannexins are a class of plasma membrane spanning proteins that presumably form a hexameric, non-selective ion channel. Although similar in secondary structure to the connexins, pannexins notably do not form endogenous gap junctions and act as bona fide ion channels. The pannexins have been primarily studied as ATP-release channels, but the overall diversity of their functions is still being elucidated. There is an intriguing theme with pannexins that has begun to develop. In this review we analyze several recent reports that converge on the idea that pannexin channels (namely Panx1) can potentiate ligand-gated receptor signaling. Although the literature remains sparse, this emerging concept appears consistent between both ionotropic and metabotropic receptors of several ligand families. Landes Bioscience 2014-03-01 2014-02-27 /pmc/articles/PMC4048300/ /pubmed/24576994 http://dx.doi.org/10.4161/chan.27978 Text en Copyright © 2014 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
spellingShingle | Review Isakson, Brant E Thompson, Roger J Pannexin-1 as a potentiator of ligand-gated receptor signaling |
title | Pannexin-1 as a potentiator of ligand-gated receptor signaling |
title_full | Pannexin-1 as a potentiator of ligand-gated receptor signaling |
title_fullStr | Pannexin-1 as a potentiator of ligand-gated receptor signaling |
title_full_unstemmed | Pannexin-1 as a potentiator of ligand-gated receptor signaling |
title_short | Pannexin-1 as a potentiator of ligand-gated receptor signaling |
title_sort | pannexin-1 as a potentiator of ligand-gated receptor signaling |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4048300/ https://www.ncbi.nlm.nih.gov/pubmed/24576994 http://dx.doi.org/10.4161/chan.27978 |
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