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

doi:10.1016/0014-5793(87)80355-1

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

Pharmacology

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	77-80
Number of pages	4
Journal	FEBS Letters
Volume	221
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(87)80355-1
State	Published - 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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10.1016/0014-5793(87)80355-1

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title = "The effect of myosin light chain phosphorylation on the actin-stimulated ATPase activity of myosin minifilaments",

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.",

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AU - Levitsky, Dmitri I.

AU - Shuvalova, Lyudmila A.

AU - Poglazov, Boris F.

PY - 1987/8/31

Y1 - 1987/8/31

N2 - 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.

AB - 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.

KW - (Rabbit skeletal muscle)

KW - ATP hydrolysis

KW - Actin-myosin interaction

KW - Myosin

KW - Phosphorylation

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

Abstract

Keywords

ASJC Scopus subject areas

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