Open AccessCalmodulin: The switch button of calcium signaling
Author(s) -
Chiu-Fen Yang,
Wen-Chin Tsai
Publication year - 2022
Publication title -
tzu-chi medical journal/cí-jì yīxué
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.343
H-Index - 15
eISSN - 2223-8956
pISSN - 1016-3190
DOI - 10.4103/tcmj.tcmj_285_20
Subject(s) - calmodulin , calcium , calcium signaling , calcium binding protein , signaling proteins , microbiology and biotechnology , linker , signal transduction , calcium in biology , biophysics , biochemistry , intracellular , biology , medicine , computer science , operating system
Calmodulin (CaM), a calcium sensor, decodes the critical calcium-dependent signals and converts them into the driving force to control various important cellular functions, such as ion transport. This small protein has a short central linker to connect two globular lobes and each unit is composed of a pair of homologous domains (HD) which are responsible for calcium binding. The conformation of each HD is sensitive to the levels of the intracellular Ca 2+ concentrations while the flexible structure of the central domain enables its interactions with hundreds of cellular proteins. Apart from calcium binding, posttranslational modifications (PTMs) also contribute to the modulations of CaM functions by affecting its protein-protein interaction networks and hence drawing out the various downstream signaling cascades. In this mini-review, we first aim to elucidate the structural features of CaM and then overview the recent studies on the engagements of calcium binding and PTMs in Ca 2+ /CaM-mediated conformational alterations and signaling events. The mechanistic understanding of CaM working models is expected to be a key to decipher the precise role of CaM in cardiac physiology and disease pathology.