Gα12 and Gα13 Interact with Ser/Thr Protein Phosphatase Type 5 and Stimulate Its Phosphatase Activity

@article{Yamaguchi2002G12AG,
  title={Gα12 and Gα13 Interact with Ser/Thr Protein Phosphatase Type 5 and Stimulate Its Phosphatase Activity},
  author={Yoshiaki Yamaguchi and H. Katoh and K. Mori and M. Negishi},
  journal={Current Biology},
  year={2002},
  volume={12},
  pages={1353-1358}
}
  • Yoshiaki Yamaguchi, H. Katoh, +1 author M. Negishi
  • Published 2002
  • Biology
  • Current Biology
  • Abstract The Gα subunits of the G 12 family of heterotrimeric G proteins, defined by Gα 12 and Gα 13 , are involved in many signaling pathways and diverse cellular functions [1]. In an attempt to elucidate downstream effectors of Gα 12 for cellular functions, we have performed a yeast two-hybrid screening of a rat brain cDNA library and revealed that Ser/Thr protein phosphatase type 5 (PP5) is a novel effector of Gα 12 and Gα 13 . PP5 is a newly identified phosphatase and consists of a C… CONTINUE READING
    95 Citations

    Figures from this paper

    Gα13 Stimulates the Tyrosine Phosphorylation of Ric-8A
    • 5
    • PDF
    Gα12 Directly Interacts with PP2A
    • 36
    • PDF
    S100 Proteins Modulate Protein Phosphatase 5 Function
    • 47
    • Highly Influenced
    • PDF
    Molecular basis for TPR domain‐mediated regulation of protein phosphatase 5
    • 182
    • PDF
    Rac GTPase signaling through the PP5 protein phosphatase.
    • 45
    • PDF

    References

    SHOWING 1-10 OF 29 REFERENCES
    The G protein Gα12 stimulates Bruton's tyrosine kinase and a rasGAP through a conserved PH/BM domain
    • 191
    The GTPase-activating Protein RGS4 Stabilizes the Transition State for Nucleotide Hydrolysis*
    • 333
    • PDF
    Signaling by the G12 class of G proteins.
    • 149
    Conformational Activation of Radixin by G13 Protein α Subunit*
    • 76
    • PDF
    A mutant alpha subunit of G12 potentiates the eicosanoid pathway and is highly oncogenic in NIH 3T3 cells.
    • 164
    • PDF
    Activation of protein phosphatase 5 by limited proteolysis or the binding of polyunsaturated fatty acids to the TPR domain
    • 130
    • Highly Influential
    Effects of serine/threonine protein phosphatases on ion channels in excitable membranes.
    • 252
    • PDF