Myosin light chain kinases

Bruce E. Kemp, James T. Stull

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations

Abstract

Ca2+ is a second messenger that activates many Ca2+-dependent cellular processes. Ca2+ has been recognized as an important component in muscle contraction and cell motility because it regulates a distinct class of protein kinases, myosin light chain kinases.1-3 Activation of myosin light chain kinase by Ca2+/calmodulin results in phosphorylation of a regulatory light chain subunit of myosin. Myosin light chain phosphorylation leads to potentiation of contraction in striated muscles, but initiates contraction in smooth muscles. Before reviewing the catalytic properties of myosin light chain kinases, a general discussion of contractile proteins and the role of myosin phosphorylation will be presented so that the reader will have some appreciation of the biological importance of this class of kinases. The main topic, however, will deal with their respective biochemical properties as elucidated with peptides.

Original languageEnglish (US)
Title of host publicationPeptides and Protein Phosphorylation
PublisherCRC Press
Pages116-133
Number of pages18
ISBN (Electronic)9781351083898
ISBN (Print)0849365309, 9781315896342
DOIs
StatePublished - Jan 1 2018

ASJC Scopus subject areas

  • Medicine(all)
  • Biochemistry, Genetics and Molecular Biology(all)

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