Distinct carboxy-termini confer divergent characteristics to the mitogen-activated protein kinase p38alpha and its splice isoform Mxi2.

@article{Sanz2000DistinctCC,
  title={Distinct carboxy-termini confer divergent characteristics to the mitogen-activated protein kinase p38alpha and its splice isoform Mxi2.},
  author={V Sanz and Imanol Arozarena and Piero Crespo},
  journal={FEBS letters},
  year={2000},
  volume={474 2-3},
  pages={169-74}
}
The p38 family of mitogen-activated protein kinases is composed of several isoforms. Mxi2 is a splicing variant of p38alpha that harbors a unique carboxy-terminus. Here we show that this sole divergence results in remarkable differences between Mxi2 and p38alpha. Mxi2 is distinctively activated by stress stimuli and potently activated by mitogens. Mxi2 affinity for bona fide p38 substrates is remarkably diminished and Mxi2 activity is largely unaffected by the phosphatase CL100. Also, Mxi2… CONTINUE READING

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