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

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

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
Externally published	Yes

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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title = "Binding of phosphorylated and dephosphorylated heavy meromyosin to F-actin",

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",

author = "Danuta Szcz{\c c}sna and Apolinary Sobieszek and Irena K{\c a}kol",

note = "Funding Information: We thank Dr J.V. Small for critical readingo f the manuscript.T he excellentt echnicala ssistance of MS U. Miiller and generala ssistanceo f Mrs G. McCoy are also acknowledgedT. heses tudiesw ere supported by a grant from the Muscular Dystrophy Association, Inc.",

year = "1987",

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doi = "10.1016/0014-5793(87)81332-7",

language = "English (US)",

volume = "210",

pages = "177--180",

journal = "FEBS Letters",

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TY - JOUR

T1 - Binding of phosphorylated and dephosphorylated heavy meromyosin to F-actin

AU - Szczçsna, Danuta

AU - Sobieszek, Apolinary

AU - Ka̧kol, Irena

N1 - Funding Information: We thank Dr J.V. Small for critical readingo f the manuscript.T he excellentt echnicala ssistance of MS U. Miiller and generala ssistanceo f Mrs G. McCoy are also acknowledgedT. heses tudiesw ere supported by a grant from the Muscular Dystrophy Association, Inc.

PY - 1987/1/5

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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U2 - 10.1016/0014-5793(87)81332-7

DO - 10.1016/0014-5793(87)81332-7

M3 - Article

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VL - 210

SP - 177

EP - 180

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2

ER -

Binding of phosphorylated and dephosphorylated heavy meromyosin to F-actin

Abstract

Keywords

ASJC Scopus subject areas

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