p38alpha is active in vitro and in vivo when monophosphorylated at threonine 180.

@article{Askari2009p38alphaIA,
  title={p38alpha is active in vitro and in vivo when monophosphorylated at threonine 180.},
  author={Nadav Askari and Jonah Beenstock and Oded Livnah and David Engelberg},
  journal={Biochemistry},
  year={2009},
  volume={48 11},
  pages={2497-504}
}
A common feature of the regulation of many protein kinases is their phosphorylation on a conserved Thr residue in the activation loop. In the family of mitogen-activated protein kinases (MAPKs), another phosphorylation event, on a Tyr residue neighboring this Thr (in a TXY motif), is required for activity. Many studies suggested that this dual phosphorylation is an absolute requirement for MAPK activation, assigning an equal role for the Thr and Tyr of the phosphorylation motif. Here we tested… CONTINUE READING

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