Overlapping Binding Sites in Protein Phosphatase 2A for Association with Regulatory A and α-4 (mTap42) Subunits*

@article{Prickett2004OverlappingBS,
  title={Overlapping Binding Sites in Protein Phosphatase 2A for Association with Regulatory A and α-4 (mTap42) Subunits*},
  author={Todd D Prickett and D. Brautigan},
  journal={Journal of Biological Chemistry},
  year={2004},
  volume={279},
  pages={38912 - 38920}
}
  • Todd D Prickett, D. Brautigan
  • Published 2004
  • Biology, Medicine
  • Journal of Biological Chemistry
  • Diverse functions of protein Ser/Thr phosphatases depend on the distribution of the catalytic subunits among multiple regulatory subunits. In cells protein phosphatase 2A catalytic subunit (PP2Ac) mostly binds to a scaffold subunit (A subunit or PR65); however, PP2Ac alternatively binds to α-4, a subunit related to yeast Tap42 protein, which also associates with phosphatases PP4 or PP6. We mapped α-4 binding to PP2Ac to the helical domain, residues 19-165. We mutated selected residues and… CONTINUE READING
    38 Citations
    Structural basis of protein phosphatase 2A stable latency
    • 45
    • PDF
    Alpha4 is an essential regulator of PP2A phosphatase activity.
    • 131

    References

    SHOWING 1-10 OF 67 REFERENCES
    Interaction between Protein Phosphatase 5 and the A subunit of Protein Phosphatase 2A
    • 57
    • PDF
    Regulation of protein phosphatase 2A catalytic activity by alpha4 protein and its yeast homolog Tap42.
    • 123
    Identification of a New Family of Protein Phosphatase 2A Regulatory Subunits (*)
    • 225
    • PDF