Post-translational regulation of cardiac myosin binding protein-C: A graphical review

被引:16
作者
Main, Alice [1 ]
Fuller, William [1 ]
Baillie, George S. [1 ]
机构
[1] Univ Glasgow, Inst Cardiovasc & Med Sci, Glasgow, Lanark, Scotland
关键词
Cardiac contractility; Cardiac myosin binding protein C; Posttranslational modification; N-TERMINAL DOMAINS; HYPERTROPHIC CARDIOMYOPATHY; DIASTOLIC DYSFUNCTION; LYSINE ACETYLATION; MASS-SPECTROMETRY; S-NITROSYLATION; F-ACTIN; MYBP-C; PHOSPHORYLATION; HEART;
D O I
10.1016/j.cellsig.2020.109788
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Cardiac myosin binding protein-C (cMyBP-C) is a fundamental component of the cardiac sarcomere involved in regulating systolic and diastolic activity, processes which must be tightly maintained to preserve cardiac function. Importantly, as a non-enzymatic protein, cMyBP-C relies solely on post-translational modifications and protein-protein interactions in order to modulate its function, and does so through phosphorylation, glutathionylation and acetylation amongst others. Although some are better understood than others, these modifications may represent novel therapeutic routes to modulate cMyBP-C function in the treatment of cardiac disease.
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页数:8
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