Activation of Myosin Light Chain Kinase Requires Translocation of Bound Calmodulin

Joanna K. Krueger, Stephen C. Gallagher, Gang Zhi, Ramaz Geguchadze, Anthony Persechini, James T. Stull, Jill Trewhella

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

A novel translocation step is inferred from structural studies of the interactions between the intracellular calcium receptor protein calmodulin (CaM) and one of its regulatory targets. A mutant of CaM missing residues 2-8 (ΔNCaM) binds skeletal muscle myosin light chain kinase with high affinity but fails to activate catalysis. Small angle x-ray scattering data reveal that ΔNCaM occupies a position near the catalytic cleft in its complex with the kinase, whereas the native protein translocates to a position near the C-terminal end of the catalytic core. Thus, CaM residues 2-8 appear to facilitate movement of bound CaM away from the vicinity of the catalytic cleft.

Original languageEnglish (US)
Pages (from-to)4535-4538
Number of pages4
JournalJournal of Biological Chemistry
Volume276
Issue number7
DOIs
StatePublished - Feb 16 2001

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Krueger, J. K., Gallagher, S. C., Zhi, G., Geguchadze, R., Persechini, A., Stull, J. T., & Trewhella, J. (2001). Activation of Myosin Light Chain Kinase Requires Translocation of Bound Calmodulin. Journal of Biological Chemistry, 276(7), 4535-4538. https://doi.org/10.1074/jbc.C000857200