Calmodulin binding to and cAMP-dependent phosphorylation of kinesin light chains modulate kinesin ATPase activity.

@article{Matthies1993CalmodulinBT,
  title={Calmodulin binding to and cAMP-dependent phosphorylation of kinesin light chains modulate kinesin ATPase activity.},
  author={Heinrich J. G. Matthies and Richard J. Miller and H. Clive Palfrey},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 15},
  pages={11176-87}
}
Kinesin is an ubiquitous heterotetrameric microtubule-based motor which translocates membrane-bound organelles. Since organelle motility and motor protein function can be regulated by components of signaling pathways, the ability of purified bovine brain kinesin (kinesin) to be phosphorylated and to recognize calmodulin (CaM) was tested. Extensively purified "kinesin" was found to consist of several forms of both heavy (KHC) and light (KLC) chains. Phosphorylation of kinesin by a variety of… CONTINUE READING

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