Distinct priming kinases contribute to differential regulation of collapsin response mediator proteins by glycogen synthase kinase-3 in vivo.

@article{Cole2006DistinctPK,
  title={Distinct priming kinases contribute to differential regulation of collapsin response mediator proteins by glycogen synthase kinase-3 in vivo.},
  author={A. A. Rush Cole and Fr{\'e}d{\'e}ric Causeret and Gokhan Yadirgi and C. James Hastie and Hilary J McLauchlan and Edward J Mcmanus and Felix Hernandez and Britta Johanna Eickholt and Margareta Nikolic and Calum Sutherland},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 24},
  pages={16591-8}
}
Collapsin response mediator proteins (CRMPs) are a family of neuron-enriched proteins that regulate neurite outgrowth and growth cone dynamics. Here, we show that Cdk5 phosphorylates CRMP1, CRMP2, and CRMP4, priming for subsequent phosphorylation by GSK3 in vitro. In contrast, DYRK2 phosphorylates and primes CRMP4 only. The Cdk5 and DYRK2 inhibitor purvalanol decreases the phosphorylation of CRMP proteins in neurons, whereas CRMP1 and CRMP2, but not CRMP4, phosphorylation is decreased in Cdk5… CONTINUE READING
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