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Physiological functions of the TRPM4 channels via protein interactions

Authors
Cho, Chang-HoonLee, Young-SunKim, EunjuHwang, Eun MiPark, Jae-Yong
Issue Date
31-1월-2015
Publisher
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
Keywords
Glycosylation; Heteromerization; Phosphorylation; SUMOylation; Trafficking; TRPM4; 14-3-gamma
Citation
BMB REPORTS, v.48, no.1, pp.1 - 5
Indexed
SCIE
SCOPUS
KCI
Journal Title
BMB REPORTS
Volume
48
Number
1
Start Page
1
End Page
5
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/94602
DOI
10.5483/BMBRep.2015.48.1.252
ISSN
1976-6696
Abstract
Transient Receptor Potential, Melastatin-related, member 4 (TRPM4) channels are Ca2+-activated Ca2+-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.
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