Vliianie fosforilirovaniia legkikh tsepeǐ miozina na vzaimodeǐstvie miozinovykh minifilamentov s F-aktinom.

Translated title of the contribution: Effect of phosphorylation of myosin light chains on the interaction of myosin minifilaments with F-actin

D. I. Levitskiǐ*, L. A. Shuvalova, P. V. Kalmykov, B. F. Poglazov

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

The effect of phosphorylation of light chains-2 (LC2) of rabbit skeletal muscle myosin on the interaction of myosin minifilaments with F-actin as well as on the actin-stimulated Mg2+-ATPase of minifilaments was studied. It was shown that in the absence of KCl the degree of F-actin-induced stimulation of myosin minifilament Mg2+-ATPase with phosphorylated LC2 exceeds 2-4-fold that with unphosphorylated LC2. Phosphorylation of LC2 considerably increases the rate of actin-stimulated Mg2+-ATPase reaction of myosin minifilaments but exerts only a very weak influence on the affinity of minifilaments for F-actin. After addition of KCl the differences in the actin-stimulated Mg2+-ATPase activity disappear in a great degree; in the presence of 50 mM KCl they do not exceed 50%. It was assumed that the observed specific influence of LC2 phosphorylation on the kinetic parameters of actin-stimulated Mg2+-ATPase reaction of myosin minifilaments is due to unique properties of the minifilaments (e.g., their ability to ordered self-assembly as a result of interaction between the heads of myosin molecules) which reflect their structural peculiarities.

Translated title of the contributionEffect of phosphorylation of myosin light chains on the interaction of myosin minifilaments with F-actin
Original languageRussian
Pages (from-to)813-824
Number of pages12
JournalBiokhimiya
Volume52
Issue number5
StatePublished - May 1 1987

ASJC Scopus subject areas

  • Chemistry(all)

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