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Related Experiment Videos

Characterization of mitotically phosphorylated caldesmon.

Y Yamakita1, S Yamashiro, F Matsumura

  • 1Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08855-1059.

The Journal of Biological Chemistry
|June 15, 1992
PubMed
Summary

Mitosis-specific phosphorylation causes caldesmon to lose its binding affinity for actin and myosin. This phosphorylation event reduces caldesmon

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Mitosis-specific phosphorylation by cdc2 kinase induces nonmuscle caldesmon dissociation from microfilaments.
  • Previous studies established the role of cdc2 kinase in caldesmon's mitotic dissociation.

Purpose of the Study:

  • To investigate the functional consequences of mitosis-specific caldesmon phosphorylation.
  • To characterize in vivo- and in vitro-phosphorylated caldesmons.

Main Methods:

  • In vivo and in vitro phosphorylation of rat non-muscle caldesmon.
  • Characterization of actin, calmodulin, and myosin binding properties.
  • Analysis of actomyosin ATPase inhibition.
  • Biochemical assays using bacterially expressed C-terminal caldesmon fragments.

Main Results:

  • Phosphorylation significantly reduces caldesmon's binding affinity for actin, calmodulin, and myosin.
  • Actin-binding constants decrease from 10^7 M-1 and 10^6 M-1 to less than 10^5 M-1 upon phosphorylation.
  • Caldesmon phosphorylation inhibits actomyosin ATPase activity.
  • A second myosin-binding site is identified in the C terminus, and its affinity is reduced by phosphorylation.

Conclusions:

  • Mitosis-specific phosphorylation of caldesmon leads to a loss of its in vitro functions.
  • These functional changes are likely crucial for microfilament reorganization during mitosis.

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