Myosin light chain kinases and myosin phosphorylation in skeletal muscle

James T. Stull; Mary H. Nunnally; Russell L. Moore; Donald K. Blumenthal

doi:10.1016/0065-2571(85)90043-3

Myosin light chain kinases and myosin phosphorylation in skeletal muscle

James T. Stull, Mary H. Nunnally, Russell L. Moore, Donald K. Blumenthal

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

36 Scopus citations

Abstract

Myosin light chain kinases appear to exist as a family of tissue- and species-specific isozymes. The skeletal muscle kinases, although differing widely in molecular weight among vertebrate species, are catalytically similar and antigenically related. The smooth muscle kinases are catalytically and antigenically distinct from the skeletal muscle kinases. The functional basis for the existence of myosin light chain kinase isozymes has not been determined. Phosphorylation of fast-twitch skeletal muscle myosin P-light chain occurs at physiologically relevant contraction frequencies and durations, and the extent of P-light chain phosphorylation correlates with enhancement of isometric twitch tension in fast-twitch muscle under a variety of experimental conditions. Phosphorylation of myosin P-light chain in vertebrate fast-twitch skeletal muscle may play a modulatory role in calcium regulation of muscle contractility.

Original language	English (US)
Pages (from-to)	123-128,IN1-IN2,129-140
Journal	Advances in Enzyme Regulation
Volume	23
Issue number	C
DOIs	https://doi.org/10.1016/0065-2571(85)90043-3
State	Published - 1985

ASJC Scopus subject areas

Molecular Medicine
Molecular Biology
Genetics
Cancer Research

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10.1016/0065-2571(85)90043-3

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title = "Myosin light chain kinases and myosin phosphorylation in skeletal muscle",

abstract = "Myosin light chain kinases appear to exist as a family of tissue- and species-specific isozymes. The skeletal muscle kinases, although differing widely in molecular weight among vertebrate species, are catalytically similar and antigenically related. The smooth muscle kinases are catalytically and antigenically distinct from the skeletal muscle kinases. The functional basis for the existence of myosin light chain kinase isozymes has not been determined. Phosphorylation of fast-twitch skeletal muscle myosin P-light chain occurs at physiologically relevant contraction frequencies and durations, and the extent of P-light chain phosphorylation correlates with enhancement of isometric twitch tension in fast-twitch muscle under a variety of experimental conditions. Phosphorylation of myosin P-light chain in vertebrate fast-twitch skeletal muscle may play a modulatory role in calcium regulation of muscle contractility.",

author = "Stull, {James T.} and Nunnally, {Mary H.} and Moore, {Russell L.} and Blumenthal, {Donald K.}",

note = "Funding Information: The research of the authors described in this manuscript was generously supported by Muscular Dystrophy Association and the National Institutes of Health (HL26096, GM09275, HL06335, and HL23990). We are grateful to Mr. Robert Blencowe for his assistance in the computer simulation and graphics involving the myosin light chain phosphorylation system in skeletal muscle.",

year = "1985",

doi = "10.1016/0065-2571(85)90043-3",

language = "English (US)",

volume = "23",

pages = "123--128,IN1--IN2,129--140",

journal = "Advances in Enzyme Regulation",

issn = "0065-2571",

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T1 - Myosin light chain kinases and myosin phosphorylation in skeletal muscle

AU - Stull, James T.

AU - Nunnally, Mary H.

AU - Moore, Russell L.

AU - Blumenthal, Donald K.

N1 - Funding Information: The research of the authors described in this manuscript was generously supported by Muscular Dystrophy Association and the National Institutes of Health (HL26096, GM09275, HL06335, and HL23990). We are grateful to Mr. Robert Blencowe for his assistance in the computer simulation and graphics involving the myosin light chain phosphorylation system in skeletal muscle.

PY - 1985

Y1 - 1985

N2 - Myosin light chain kinases appear to exist as a family of tissue- and species-specific isozymes. The skeletal muscle kinases, although differing widely in molecular weight among vertebrate species, are catalytically similar and antigenically related. The smooth muscle kinases are catalytically and antigenically distinct from the skeletal muscle kinases. The functional basis for the existence of myosin light chain kinase isozymes has not been determined. Phosphorylation of fast-twitch skeletal muscle myosin P-light chain occurs at physiologically relevant contraction frequencies and durations, and the extent of P-light chain phosphorylation correlates with enhancement of isometric twitch tension in fast-twitch muscle under a variety of experimental conditions. Phosphorylation of myosin P-light chain in vertebrate fast-twitch skeletal muscle may play a modulatory role in calcium regulation of muscle contractility.

AB - Myosin light chain kinases appear to exist as a family of tissue- and species-specific isozymes. The skeletal muscle kinases, although differing widely in molecular weight among vertebrate species, are catalytically similar and antigenically related. The smooth muscle kinases are catalytically and antigenically distinct from the skeletal muscle kinases. The functional basis for the existence of myosin light chain kinase isozymes has not been determined. Phosphorylation of fast-twitch skeletal muscle myosin P-light chain occurs at physiologically relevant contraction frequencies and durations, and the extent of P-light chain phosphorylation correlates with enhancement of isometric twitch tension in fast-twitch muscle under a variety of experimental conditions. Phosphorylation of myosin P-light chain in vertebrate fast-twitch skeletal muscle may play a modulatory role in calcium regulation of muscle contractility.

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DO - 10.1016/0065-2571(85)90043-3

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SP - 123-128,IN1-IN2,129-140

JO - Advances in Enzyme Regulation

JF - Advances in Enzyme Regulation

IS - C

ER -

Myosin light chain kinases and myosin phosphorylation in skeletal muscle

Abstract

ASJC Scopus subject areas

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