Physiological functions of the TRPM4 channels via protein interactions
- Authors
- Cho, Chang-Hoon; Lee, Young-Sun; Kim, Eunju; Hwang, Eun Mi; Park, 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.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - College of Health Sciences > School of Biosystems and Biomedical Sciences > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.