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Physiological functions of the TRPM4 channels via protein interactions

Transient Receptor Potential, Melastatin-related, member 4 (TRPM4) channels are Ca(2+)-activated Ca(2+)-impermeable cation channels. These channels are expressed in various types of mammalian tissues including the brain and are implicated in many diverse physiological and pathophysiological conditio...

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Autores principales: Cho, Chang-Hoon, Lee, Young-Sun, Kim, Eunju, Hwang, Eun Mi, Park, Jae-Yong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Korean Society for Biochemistry and Molecular Biology 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4345635/
https://www.ncbi.nlm.nih.gov/pubmed/25441424
http://dx.doi.org/10.5483/BMBRep.2015.48.1.252
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author Cho, Chang-Hoon
Lee, Young-Sun
Kim, Eunju
Hwang, Eun Mi
Park, Jae-Yong
author_facet Cho, Chang-Hoon
Lee, Young-Sun
Kim, Eunju
Hwang, Eun Mi
Park, Jae-Yong
author_sort Cho, Chang-Hoon
collection PubMed
description Transient Receptor Potential, Melastatin-related, member 4 (TRPM4) channels are Ca(2+)-activated Ca(2+)-impermeable cation channels. These channels are expressed in various types of mammalian tissues including the brain and are implicated in many diverse physiological and pathophysiological conditions. In the past several years, the trafficking processes and regulatory mechanism of these channels and their interacting proteins have been uncovered. Here in this minireview, we summarize the current understanding of the trafficking mechanism of TRPM4 channels on the plasma membrane as well as heteromeric complex formation via protein interactions. We also describe physiological implications of protein-TRPM4 interactions and suggest TRPM4 channels as therapeutic targets in many related diseases. [BMB Reports 2015; 48(1): 1-5]
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spelling pubmed-43456352015-03-02 Physiological functions of the TRPM4 channels via protein interactions Cho, Chang-Hoon Lee, Young-Sun Kim, Eunju Hwang, Eun Mi Park, Jae-Yong BMB Rep Invited Mini Review Transient Receptor Potential, Melastatin-related, member 4 (TRPM4) channels are Ca(2+)-activated Ca(2+)-impermeable cation channels. These channels are expressed in various types of mammalian tissues including the brain and are implicated in many diverse physiological and pathophysiological conditions. In the past several years, the trafficking processes and regulatory mechanism of these channels and their interacting proteins have been uncovered. Here in this minireview, we summarize the current understanding of the trafficking mechanism of TRPM4 channels on the plasma membrane as well as heteromeric complex formation via protein interactions. We also describe physiological implications of protein-TRPM4 interactions and suggest TRPM4 channels as therapeutic targets in many related diseases. [BMB Reports 2015; 48(1): 1-5] Korean Society for Biochemistry and Molecular Biology 2015-01 /pmc/articles/PMC4345635/ /pubmed/25441424 http://dx.doi.org/10.5483/BMBRep.2015.48.1.252 Text en Copyright © 2015, Korean Society for Biochemistry and Molecular Biology http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Invited Mini Review
Cho, Chang-Hoon
Lee, Young-Sun
Kim, Eunju
Hwang, Eun Mi
Park, Jae-Yong
Physiological functions of the TRPM4 channels via protein interactions
title Physiological functions of the TRPM4 channels via protein interactions
title_full Physiological functions of the TRPM4 channels via protein interactions
title_fullStr Physiological functions of the TRPM4 channels via protein interactions
title_full_unstemmed Physiological functions of the TRPM4 channels via protein interactions
title_short Physiological functions of the TRPM4 channels via protein interactions
title_sort physiological functions of the trpm4 channels via protein interactions
topic Invited Mini Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4345635/
https://www.ncbi.nlm.nih.gov/pubmed/25441424
http://dx.doi.org/10.5483/BMBRep.2015.48.1.252
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