Absolute quantification of multisite phosphorylation by selective reaction monitoring mass spectrometry: determination of inhibitory phosphorylation status of cyclin-dependent kinases.

@article{Mayya2006AbsoluteQO,
  title={Absolute quantification of multisite phosphorylation by selective reaction monitoring mass spectrometry: determination of inhibitory phosphorylation status of cyclin-dependent kinases.},
  author={Viveka Mayya and Karim Rezual and Linfeng Wu and Michael B Fong and David K. Han},
  journal={Molecular & cellular proteomics : MCP},
  year={2006},
  volume={5 6},
  pages={1146-57}
}
Multisite phosphorylation is an important mechanism for achieving intricate regulation of protein function. Here we extended the absolute quantification of abundance (AQUA) methodology and validated its applicability to quantitatively study multisite phosphorylation. As a test case, we chose the conserved inhibitory site of the cyclin-dependent kinases (CDKs), Cdk1, Cdk2, and Cdk3, which are important regulators of cell cycle transitions and apoptosis. Inhibitory phosphorylation at Thr(14) and… CONTINUE READING