Physiological functions of the TRPM4 channels via protein interactions

被引：22
作者：
Cho, Chang-Hoon [1 ]
Lee, Young-Sun [2 ,3 ,4 ]
Kim, Eunju [1 ,2 ]
Hwang, Eun Mi [2 ,5 ]
Park, Jae-Yong [1 ]
机构：
[1] Korea Univ, Sch Biosyst & Biomed Sci, Coll Hlth Sci, Seoul 136703, South Korea
[2] Korea Inst Sci & Technol, Ctr Funct Connect, Seoul 136791, South Korea
[3] Gyeongsang Natl Univ, Inst Hlth Sci, Dept Physiol, Sch Med, Jinju 660751, South Korea
[4] Gyeongsang Natl Univ, Med Res Ctr Neural Dysfunct, Sch Med, Jinju 660751, South Korea
[5] Univ Sci & Technol, Neurosci Program, Taejon 305350, South Korea
来源：
BMB REPORTS | 2015年 / 48卷 / 01期
基金：
新加坡国家研究基金会;
关键词：
Glycosylation; Heteromerization; Phosphorylation; SUMOylation; Trafficking; TRPM4; 14-3-gamma; GATED ION CHANNELS; NEUROTRANSMITTER RECEPTORS; GLYCOSYLATION; TRAFFICKING; MELASTATIN; PHOSPHORYLATION; MODULATION; EXPRESSION; NEURONS; CELLS;
D O I：
10.5483/BMBRep.2015.48.1.252
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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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收藏
页码：1 / 5
页数：5
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