Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1.

@article{Robinson2002IdentificationON,
  title={Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1.},
  author={Fred L Robinson and Angelique Whitehurst and Malavika Raman and Melanie H Cobb},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 17},
  pages={14844-52}
}
Extracellular signal-regulated kinases 1 and 2 (ERK1 and ERK2) are essential components of pathways through which signals received at membrane receptors are converted into specific changes in protein function and gene expression. As with other members of the mitogen-activated protein (MAP) kinase family, ERK1 and ERK2 are activated by phosphorylations catalyzed by dual-specificity protein kinases known as MAP/ERK kinases (MEKs). MEKs exhibit stringent specificity for individual MAP kinases… CONTINUE READING