Phosphorylation of the ARE-binding protein DAZAP1 by ERK2 induces its dissociation from DAZ.

@article{Morton2006PhosphorylationOT,
  title={Phosphorylation of the ARE-binding protein DAZAP1 by ERK2 induces its dissociation from DAZ.},
  author={Simon Morton and Huei-Ting Yang and Ntsane Moleleki and David G. Campbell and Philip Cohen and Simon Rousseau},
  journal={The Biochemical journal},
  year={2006},
  volume={399 2},
  pages={
          265-73
        }
}
A protein in RAW 264.7 macrophages, which became phosphorylated in response to LPS (lipopolysaccharide), was identified as the RNA-binding protein called DAZAP1 [DAZ (deleted in azoospermia)-associated protein 1]. The phosphorylation of this protein was prevented by specific inhibition of MKK1 [MAPK (mitogen-activated protein kinase) kinase 1], indicating that it was phosphorylated via the classical MAPK cascade. Further experiments showed that DAZAP1 was phosphorylated stoichiometrically in… 

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