Myosin light chain kinases

Bruce E. Kemp, James T. Stull

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Citation (Scopus)

Abstract

Ca2+ is a second messenger that activates many Ca2+-dependent cellular processes. Ca2+ has been recognized as an important component in muscle contraction and cell motility because it regulates a distinct class of protein kinases, myosin light chain kinases.1-3 Activation of myosin light chain kinase by Ca2+/calmodulin results in phosphorylation of a regulatory light chain subunit of myosin. Myosin light chain phosphorylation leads to potentiation of contraction in striated muscles, but initiates contraction in smooth muscles. Before reviewing the catalytic properties of myosin light chain kinases, a general discussion of contractile proteins and the role of myosin phosphorylation will be presented so that the reader will have some appreciation of the biological importance of this class of kinases. The main topic, however, will deal with their respective biochemical properties as elucidated with peptides.

Original languageEnglish (US)
Title of host publicationPeptides and Protein Phosphorylation
PublisherCRC Press
Pages116-133
Number of pages18
ISBN (Electronic)9781351083898
ISBN (Print)0849365309, 9781315896342
DOIs
StatePublished - Jan 1 2018

Fingerprint

Myosin-Light-Chain Kinase
Myosin Light Chains
Phosphorylation
Muscle
Myosins
Muscle Contraction
Contractile Proteins
Striated Muscle
Second Messenger Systems
Calmodulin
Protein Kinases
Muscle Cells
Cell Movement
Smooth Muscle
Phosphotransferases
Chemical activation
Peptides

ASJC Scopus subject areas

  • Medicine(all)
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Kemp, B. E., & Stull, J. T. (2018). Myosin light chain kinases. In Peptides and Protein Phosphorylation (pp. 116-133). CRC Press. https://doi.org/10.1201/9781351075442

Myosin light chain kinases. / Kemp, Bruce E.; Stull, James T.

Peptides and Protein Phosphorylation. CRC Press, 2018. p. 116-133.

Research output: Chapter in Book/Report/Conference proceedingChapter

Kemp, BE & Stull, JT 2018, Myosin light chain kinases. in Peptides and Protein Phosphorylation. CRC Press, pp. 116-133. https://doi.org/10.1201/9781351075442
Kemp BE, Stull JT. Myosin light chain kinases. In Peptides and Protein Phosphorylation. CRC Press. 2018. p. 116-133 https://doi.org/10.1201/9781351075442
Kemp, Bruce E. ; Stull, James T. / Myosin light chain kinases. Peptides and Protein Phosphorylation. CRC Press, 2018. pp. 116-133
@inbook{6994eca502e24ebd885fb6dbb2e42234,
title = "Myosin light chain kinases",
abstract = "Ca2+ is a second messenger that activates many Ca2+-dependent cellular processes. Ca2+ has been recognized as an important component in muscle contraction and cell motility because it regulates a distinct class of protein kinases, myosin light chain kinases.1-3 Activation of myosin light chain kinase by Ca2+/calmodulin results in phosphorylation of a regulatory light chain subunit of myosin. Myosin light chain phosphorylation leads to potentiation of contraction in striated muscles, but initiates contraction in smooth muscles. Before reviewing the catalytic properties of myosin light chain kinases, a general discussion of contractile proteins and the role of myosin phosphorylation will be presented so that the reader will have some appreciation of the biological importance of this class of kinases. The main topic, however, will deal with their respective biochemical properties as elucidated with peptides.",
author = "Kemp, {Bruce E.} and Stull, {James T.}",
year = "2018",
month = "1",
day = "1",
doi = "10.1201/9781351075442",
language = "English (US)",
isbn = "0849365309",
pages = "116--133",
booktitle = "Peptides and Protein Phosphorylation",
publisher = "CRC Press",

}

TY - CHAP

T1 - Myosin light chain kinases

AU - Kemp, Bruce E.

AU - Stull, James T.

PY - 2018/1/1

Y1 - 2018/1/1

N2 - Ca2+ is a second messenger that activates many Ca2+-dependent cellular processes. Ca2+ has been recognized as an important component in muscle contraction and cell motility because it regulates a distinct class of protein kinases, myosin light chain kinases.1-3 Activation of myosin light chain kinase by Ca2+/calmodulin results in phosphorylation of a regulatory light chain subunit of myosin. Myosin light chain phosphorylation leads to potentiation of contraction in striated muscles, but initiates contraction in smooth muscles. Before reviewing the catalytic properties of myosin light chain kinases, a general discussion of contractile proteins and the role of myosin phosphorylation will be presented so that the reader will have some appreciation of the biological importance of this class of kinases. The main topic, however, will deal with their respective biochemical properties as elucidated with peptides.

AB - Ca2+ is a second messenger that activates many Ca2+-dependent cellular processes. Ca2+ has been recognized as an important component in muscle contraction and cell motility because it regulates a distinct class of protein kinases, myosin light chain kinases.1-3 Activation of myosin light chain kinase by Ca2+/calmodulin results in phosphorylation of a regulatory light chain subunit of myosin. Myosin light chain phosphorylation leads to potentiation of contraction in striated muscles, but initiates contraction in smooth muscles. Before reviewing the catalytic properties of myosin light chain kinases, a general discussion of contractile proteins and the role of myosin phosphorylation will be presented so that the reader will have some appreciation of the biological importance of this class of kinases. The main topic, however, will deal with their respective biochemical properties as elucidated with peptides.

UR - http://www.scopus.com/inward/record.url?scp=85053094485&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85053094485&partnerID=8YFLogxK

U2 - 10.1201/9781351075442

DO - 10.1201/9781351075442

M3 - Chapter

AN - SCOPUS:85053094485

SN - 0849365309

SN - 9781315896342

SP - 116

EP - 133

BT - Peptides and Protein Phosphorylation

PB - CRC Press

ER -