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- W3195784048 abstract "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 Ca2+ 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 Ca2+/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." @default.
- W3195784048 created "2021-08-30" @default.
- W3195784048 creator A5058249899 @default.
- W3195784048 creator A5081508699 @default.
- W3195784048 date "2022-01-01" @default.
- W3195784048 modified "2023-09-25" @default.
- W3195784048 title "Calmodulin: The switch button of calcium signaling" @default.
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- W3195784048 doi "https://doi.org/10.4103/tcmj.tcmj_285_20" @default.
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- W3195784048 hasPublicationYear "2022" @default.
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