Direct evidence for tyrosine and threonine phosphorylation and activation of mitogen-activated protein kinase by vasopressin in cultured rat vascular smooth muscle cells.

@article{Granot1993DirectEF,
  title={Direct evidence for tyrosine and threonine phosphorylation and activation of mitogen-activated protein kinase by vasopressin in cultured rat vascular smooth muscle cells.},
  author={Yossef Granot and Eleanor Erikson and Herv{\'e} W. Fridman and Vicki Van Putten and Belinda Williams and Robert Schrier and James L. Maller},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 13},
  pages={9564-9}
}
Mitogen-activated protein (MAP) kinases are members of a 40-45-kDa family of serine/threonine protein kinases that phosphorylate several substrates including microtubule-associated protein-2, S6 kinase, and myelin basic protein. Activity of MAP kinases is regulated by growth factors that stimulate the phosphorylation of threonine 188 and tyrosine 190 in the kinase. In this paper direct evidence is presented for tyrosine and threonine phosphorylation of MAP kinase in concert with elevated… CONTINUE READING

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