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- W1420121388 abstract "This chapter examines the role of autophosphorylation in the potential regulation of protein kinases. Many of the Ca2+-mediated processes are coupled to calmodulin, a ubiquitous Ca2+-binding protein, and specific protein kinases whose activities are regulated in a Ca2+/calmodulin-dependent manner. Many of these protein kinases undergo autophosphorylation—that is, the holoenzyme catalyzes the phosphorylation of one or more amino acids within its own structure through an intramolecular reaction. Moreover, autophosphorylation is an important event in regulating kinase function(s) in vivo. Phosphorylase kinase, myosin light chain kinase (MLCK), and multifunctional calmodulin-dependent protein kinase are regulated by Ca2+/calmodulin and display autophosphorylation. The analysis of the function of specific subunits of phosphorylase kinase is also outlined. The determinants of substrate specificity of phosphorylase kinase are elucidated by kinetic studies, using synthetic peptides corresponding to the site phosphorylated in phosphorylase B as substrates. Autophosphorylation of multiple sites also plays a useful role in controlling MLCK activity of by modulating the reversal by protein phosphatases." @default.
- W1420121388 created "2016-06-24" @default.
- W1420121388 creator A5026531925 @default.
- W1420121388 creator A5060827101 @default.
- W1420121388 date "1987-01-01" @default.
- W1420121388 modified "2023-10-14" @default.
- W1420121388 title "[52] Role of autophosphorylation in regulating calmodulin-dependent protein kinases" @default.
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- W1420121388 doi "https://doi.org/10.1016/0076-6879(87)39121-9" @default.
- W1420121388 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3587043" @default.
- W1420121388 hasPublicationYear "1987" @default.
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