Binding of phosphorylated and dephosphorylated heavy meromyosin to F-actin

Danuta Szczçsna; Apolinary Sobieszek; Irena Ka̧kol

doi:10.1016/0014-5793(87)81332-7

Binding of phosphorylated and dephosphorylated heavy meromyosin to F-actin

Danuta Szczçsna, Apolinary Sobieszek, Irena Ka̧kol

Molecular and Cellular Pharmacology

Research output: Contribution to journal › Article

8 Scopus citations

Abstract

The effect of myosin light chain phosphorylation in skeletal muscle was investigated with respect to the binding affinity of phosphorylated and dephosphorylated heavy meromyosin (HMM) for F-actin in the absence of ATP. For phosphorylated HMM the affinity was 2.5-times weaker in the presence of Ca²⁺ as in its absence (HMM divalent binding sites saturated only with Mg). For dephosphorylated HMM the reverse was true, the binding being 2.4-times higher in the presence of Ca²⁺.

Original language	English (US)
Pages (from-to)	177-180
Number of pages	4
Journal	FEBS letters
Volume	210
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(87)81332-7
State	Published - Jan 5 1987

Keywords

(Skeletal muscle)
Actin binding
Dephosphorylation
Meromyosin
Phosphorylation

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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10.1016/0014-5793(87)81332-7

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Szczçsna, D., Sobieszek, A., & Ka̧kol, I. (1987). Binding of phosphorylated and dephosphorylated heavy meromyosin to F-actin. FEBS letters, 210(2), 177-180. https://doi.org/10.1016/0014-5793(87)81332-7

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abstract = "The effect of myosin light chain phosphorylation in skeletal muscle was investigated with respect to the binding affinity of phosphorylated and dephosphorylated heavy meromyosin (HMM) for F-actin in the absence of ATP. For phosphorylated HMM the affinity was 2.5-times weaker in the presence of Ca2+ as in its absence (HMM divalent binding sites saturated only with Mg). For dephosphorylated HMM the reverse was true, the binding being 2.4-times higher in the presence of Ca2+.",

keywords = "(Skeletal muscle), Actin binding, Dephosphorylation, Meromyosin, Phosphorylation",

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AU - Szczçsna, Danuta

AU - Sobieszek, Apolinary

AU - Ka̧kol, Irena

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Y1 - 1987/1/5

N2 - The effect of myosin light chain phosphorylation in skeletal muscle was investigated with respect to the binding affinity of phosphorylated and dephosphorylated heavy meromyosin (HMM) for F-actin in the absence of ATP. For phosphorylated HMM the affinity was 2.5-times weaker in the presence of Ca2+ as in its absence (HMM divalent binding sites saturated only with Mg). For dephosphorylated HMM the reverse was true, the binding being 2.4-times higher in the presence of Ca2+.

AB - The effect of myosin light chain phosphorylation in skeletal muscle was investigated with respect to the binding affinity of phosphorylated and dephosphorylated heavy meromyosin (HMM) for F-actin in the absence of ATP. For phosphorylated HMM the affinity was 2.5-times weaker in the presence of Ca2+ as in its absence (HMM divalent binding sites saturated only with Mg). For dephosphorylated HMM the reverse was true, the binding being 2.4-times higher in the presence of Ca2+.

KW - (Skeletal muscle)

KW - Actin binding

KW - Dephosphorylation

KW - Meromyosin

KW - Phosphorylation

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