Protein phosphatase 2A holoenzyme assembly: identification of contacts between B-family regulatory and scaffolding A subunits.

@article{Strack2002ProteinP2,
  title={Protein phosphatase 2A holoenzyme assembly: identification of contacts between B-family regulatory and scaffolding A subunits.},
  author={Stefan Strack and Ralf Ruediger and Gernot Walter and Ruben K Dagda and Chris A Barwacz and J. Thomas Cribbs},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 23},
  pages={20750-5}
}
Protein serine/threonine phosphatase (PP) 2A is a ubiquitous enzyme with pleiotropic functions. Trimeric PP2A consists of a structural A subunit, a catalytic C subunit, and a variable regulatory subunit. Variable subunits (B, B', and B" families) dictate PP2A substrate specificity and subcellular localization. B-family subunits contain seven WD repeats predicted to fold into a beta-propeller structure. We carried out mutagenesis of Bgamma to identify domains important for association with A and… CONTINUE READING

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