Structural requirements for phosphorylation of myosin regulatory light chain from smooth muscle

Gang Zhi, B. Herring, James T. Stull

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Site-directed and chimeric mutations of myosin regulatory light chains were used to identify residues important for phosphorylation of Ser19 by smooth muscle myosin light chain kinase. Arg16 and hydrophobic residues C- terminal of Ser19 in smooth muscle light chain were important substrate determinants in the intact protein. However, changes in the kinetic properties with mutations in the light chain were substantially smaller than results reported with structurally similar synthetic peptide substrates. These results together with the low V(max) value for short peptide substrates containing the consensus phosphorylation sequence suggest that there may be additional sites of interactions between the kinase and protein substrate. Chimeras of skeletal and smooth muscle light chains were constructed with exchanges at the N terminus and subdomains I, II, III, and IV. Analysis of results obtained on the kinetic properties for phosphorylation showed that subdomains I and II contribute to high V(max) values. Thus, a region distant from the consensus phosphorylation sequence in smooth muscle light chain is also an important substrate determinant for myosin light chain kinase.

Original languageEnglish
Pages (from-to)24723-24727
Number of pages5
JournalJournal of Biological Chemistry
Volume269
Issue number40
StatePublished - Oct 7 1994

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Myosin Light Chains
Phosphorylation
Smooth Muscle
Muscle
Myosin-Light-Chain Kinase
Light
Consensus Sequence
Substrates
Smooth Muscle Myosins
Peptides
Mutation
Kinetics
Protein Kinases
Skeletal Muscle
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Structural requirements for phosphorylation of myosin regulatory light chain from smooth muscle. / Zhi, Gang; Herring, B.; Stull, James T.

In: Journal of Biological Chemistry, Vol. 269, No. 40, 07.10.1994, p. 24723-24727.

Research output: Contribution to journalArticle

Zhi, Gang ; Herring, B. ; Stull, James T. / Structural requirements for phosphorylation of myosin regulatory light chain from smooth muscle. In: Journal of Biological Chemistry. 1994 ; Vol. 269, No. 40. pp. 24723-24727.
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