The effect of myosin light chain phosphorylation on the actin-stimulated ATPase activity of myosin minifilaments

Dmitri I. Levitsky*, Lyudmila A. Shuvalova, Boris F. Poglazov

*Corresponding author for this work

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

It has been shown that in the absence of KCl, the actin-stimulated Mg2+-ATPase activity of rabbit skeletal myosin minifilaments with phosphorylated regulatory lights chains (LC2) exceeds 3-4-fold that of myosin minifilaments with dephosphorylated LC2. Addition of KCl leads to a decrease in the difference between the two ATPase activities. LC2 phosphorylation considerably increases the rate of ATPase reaction and only slightly decreases the affinity of myosin minifilaments for F-actin. It is suggested that the unusual effect of LC2 phosphorylation on the kinetic parameters of the actin-stimulated ATPase reaction of myosin minifilaments can be accounted for by its influence on the interaction between myosin heads which results in the ordered self-assembly of minifilaments.

Original languageEnglish (US)
Pages (from-to)77-80
Number of pages4
JournalFEBS Letters
Volume221
Issue number1
DOIs
StatePublished - Aug 31 1987

Keywords

  • (Rabbit skeletal muscle)
  • ATP hydrolysis
  • Actin-myosin interaction
  • Myosin
  • Phosphorylation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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