Characterization of a domain that transiently converts class 2 DYRKs into intramolecular tyrosine kinases.

@article{Kinstrie2010CharacterizationOA,
  title={Characterization of a domain that transiently converts class 2 DYRKs into intramolecular tyrosine kinases.},
  author={Ross Kinstrie and Nathan Luebbering and Diego Miranda-Saavedra and Gary J. Sibbet and Jingfen Han and Pamela A. Lochhead and Vaughn Cleghon},
  journal={Science signaling},
  year={2010},
  volume={3 111},
  pages={ra16}
}
Dual-specificity tyrosine phosphorylation-regulated kinases (DYRKs) autophosphorylate an essential tyrosine residue in their activation loop and phosphorylate their substrates on serine and threonine residues. Phosphorylation of the activation loop tyrosine occurs intramolecularly, is mediated by a short-lived transitional intermediate during protein maturation, and is required for functional serine-threonine kinase activity of DYRKs. The DYRK family is separated into two subclasses. Through… CONTINUE READING

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