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
    View on ASBMB
    jbc.org
    38 Citations
    Background Citations
    19
    Methods Citations
    2
    38 Citations
    Citation Type

    Citation Type

    Mapping of protein phosphatase-6 association with its SAPS domain regulatory subunit using a model of helical repeats
    • 17
    The α4 Regulatory Subunit Exerts Opposing Allosteric Effects on Protein Phosphatases PP6 and PP2A*
    • 92
    • PDF
    The E3 Ubiquitin Ligase- and Protein Phosphatase 2A (PP2A)-binding Domains of the Alpha4 Protein Are Both Required for Alpha4 to Inhibit PP2A Degradation*
    • 43
    • PDF
    Structural basis of protein phosphatase 2A stable latency
    • 45
    • PDF
    Interaction analysis of the heterotrimer formed by the phosphatase 2A catalytic subunit, α4 and the mammalian ortholog of yeast Tip41 (TIPRL)
    • 33
    NMR Studies of the C-Terminus of alpha4 Reveal Possible Mechanism of Its Interaction with MID1 and Protein Phosphatase 2A
    • 6
    • PDF
    The biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificity
    • 135
    Protein Phosphatase 6 Subunit with Conserved Sit4-associated Protein Domain Targets IκBϵ*
    • 78
    • PDF
    Alpha4 is an essential regulator of PP2A phosphatase activity.
    • 131
    Low resolution structure of the human α4 protein (IgBP1) and studies on the stability of α4 and of its yeast ortholog Tap42
    • 18

    References

    SHOWING 1-10 OF 67 REFERENCES
    Interaction between Protein Phosphatase 5 and the A subunit of Protein Phosphatase 2A
    • 57
    • PDF
    Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1
    • 567
    Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the alpha 4 subunit which promotes dephosphorylation of elongation factor-2.
    • 90
    Active-site mutations impairing the catalytic function of the catalytic subunit of human protein phosphatase 2A permit baculovirus-mediated overexpression in insect cells.
    • 42
    • PDF
    The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1.
    • 75
    • PDF
    Modulation of the enzymatic properties of protein phosphatase 2A catalytic subunit by the recombinant 65-kDa regulatory subunit PR65alpha.
    • 70
    Protein phosphatase 2A subunit assembly: the catalytic subunit carboxy terminus is important for binding cellular B subunit but not polyomavirus middle tumor antigen
    • 123
    • 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
    B cell receptor-associated protein α4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A
    • 201
    • PDF