The structure of Tap42/alpha4 reveals a tetratricopeptide repeat-like fold and provides insights into PP2A regulation.

@article{Yang2007TheSO,
  title={The structure of Tap42/alpha4 reveals a tetratricopeptide repeat-like fold and provides insights into PP2A regulation.},
  author={Jing Yang and Stephen Mark Roe and Todd Prickett and David L. Brautigan and David Barford},
  journal={Biochemistry},
  year={2007},
  volume={46 30},
  pages={
          8807-15
        }
}
Physiological functions of protein phosphatase 2A (PP2A) are determined via the association of its catalytic subunit (PP2Ac) with diverse regulatory subunits. The predominant form of PP2Ac assembles into a heterotrimer comprising the scaffolding PR65/A subunit together with a variable regulatory B subunit. A distinct population of PP2Ac associates with the Tap42/alpha4 subunit, an interaction mutually exclusive with that of PR65/A. Tap42/alpha4 is also an interacting subunit of the PP2Ac… CONTINUE READING
BETA

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