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The G protein Gα12 stimulates Bruton's tyrosine kinase and a rasGAP through a conserved PH/BM domain

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Listed:
  • Yun Jiang

    (Cornell University Medical College)

  • Wei Ma

    (Cornell University Medical College)

  • Yong Wan

    (Cornell University Medical College)

  • Tohru Kozasa

    (University of Texas Southwestern Medical Center)

  • Seisuke Hattori

    (National Institute of Neuroscience)

  • Xin-Yun Huang

    (Cornell University Medical College)

Abstract

Heterotrimeric guanine-nucleotide-binding proteins (G proteins) are signal transducers that relay messages from many receptors on the cell surface to modulate various cellular processes1,2,3,4. The direct downstream effectors of G proteins consist of the signalling molecules that are activated by their physical interactions with a Gα or Gβγ subunit. Effectors that interact directly with Gα12 G proteins have yet to be identified5,6. Here we show that Gα12 binds directly to, and stimulates the activity of, Bruton's tyrosine kinase (Btk) and a Ras GTPase-activating protein, Gap1m, in vitro and in vivo. Gα12 interacts with a conserved domain, composed of the pleckstrin-homology domain and the adjacent Btk motif, that is present in both Btk and Gap1m. Our results are, to our knowledge, the first to identify direct effectors for Gα12 and to show that there is a direct link between heterotrimeric and monomeric G proteins.

Suggested Citation

  • Yun Jiang & Wei Ma & Yong Wan & Tohru Kozasa & Seisuke Hattori & Xin-Yun Huang, 1998. "The G protein Gα12 stimulates Bruton's tyrosine kinase and a rasGAP through a conserved PH/BM domain," Nature, Nature, vol. 395(6704), pages 808-813, October.
    • Handle: RePEc:nat:nature:v:395:y:1998:i:6704:d:10.1038_27454
    DOI: 10.1038/27454
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