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J Biol Chem, Vol. 275, Issue 4, 2255-2258, January 28, 2000

ACCELERATED PUBLICATION
Association of Heterotrimeric G_i with the Insulin-like Growth Factor-I Receptor
RELEASE OF G SUBUNITS UPON RECEPTOR ACTIVATION^*

Hazem Hallak, Andrea E. M. Seiler, Jaime S. Green, Brian N. Ross, and Raphael Rubin

From the Department of Pathology, Anatomy and Cell Biology, Jefferson Medical College, Philadelphia, Pennsylvania 19107

The insulin-like growth factor-I receptor (IGF-IR) is a key regulator of cell proliferation and survival. Activation of the IGF-IR induces tyrosine autophosphorylation and the binding of a series of adaptor molecules, thereby leading to the activation of MAPK. It has been demonstrated that pertussis toxin, which inactivates the G_i class of GTP-binding proteins, inhibits IGF-I-mediated activation of MAPK, and a specific role for G subunits in IGF-I signaling was shown. In the present study, we have investigated the role of heterotrimeric G_i in IGF-IR signaling in neuronal cells. Pertussis toxin inhibited IGF-I-induced activation of MAPK in rat cerebellar granule neurons and NG-108 neuronal cells. G_i and G subunits were associated with IGF-IR immunoprecipitates. Similarly, in IGF-IR-null mouse embryo fibroblasts transfected with the human IGF-IR, G_i was complexed with the IGF-IR. G_s was not associated with the IGF-IR in any cell type. IGF-I induced the release of the G subunits from the IGF-IR but had no effect on the association of G_i. These results demonstrate an association of heterotrimeric G_i with the IGF-IR and identify a discrete pool of G subunits available for downstream signaling following stimulation with IGF-I.

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