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Science 20 June 1997:
Vol. 276. no. 5320, pp. 1878 - 1881
DOI: 10.1126/science.276.5320.1878
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Reports

Activation of the G Protein Gq/11 Through Tyrosine Phosphorylation of the alpha  Subunit

Hisashi Umemori, Takafumi Inoue, Shoen Kume, Naohiro Sekiyama, Motoshi Nagao, Hiroshi Itoh, Shigetada Nakanishi, Katsuhiko Mikoshiba, Tadashi Yamamoto

Various receptors coupled to the heterotrimeric guanine nucleotide-binding protein Gq/11 stimulate formation of inositol-1,4,5-trisphosphate (IP3). Activation of these receptors also induces protein tyrosine phosphorylation. Formation of IP3 in response to stimulated receptors that couple to Gq/11 was blocked by protein tyrosine kinase inhibitors. These inhibitors appeared to act before activation of Gq/11. Moreover, stimulation of receptors coupled to Gq/11 induced phosphorylation on a tyrosine residue (Tyr356) of the Galpha q/11 subunit, and this tyrosine phosphorylation event was essential for Gq/11 activation. Tyrosine phosphorylation of Galpha q/11 induced changes in its interaction with receptors. Therefore, tyrosine phosphorylation of Galpha q/11 appears to regulate the activation of Gq/11 protein.

H. Umemori and T. Yamamoto, Department of Oncology, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan.
T. Inoue, S. Kume, K. Mikoshiba, Department of Molecular Neurobiology, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan.
N. Sekiyama and S. Nakanishi, Department of Biological Sciences, Kyoto University Faculty of Medicine, Kyoto 606, Japan.
M. Nagao and H. Itoh, Department of Biological Sciences, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226, Japan.

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