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(Received for publication, April 15, 1996, and in revised form, May 23, 1996)
From the We have utilized the yeast two-hybrid system to
identify proteins that interact with the cytoplasmic domain of the
insulin receptor. We identified a human cDNA that is a splice
variant of the human GRB10 homolog GRB-IR, which we term GRB10/IR-SV1
(for GRB10/GRB-IR splice variant 1). The protein encoded by the
GRB10/IR-SV1 cDNA contains an SH2 domain and a pleckstrin homology
domain. Cloning of a full-length human cDNA revealed a predicted
coding sequence that was similar to the mouse GRB10 protein, although
GRB10/IR-SV1 contained an 80-amino acid deletion. The GRB10/IR-SV1
cDNA is a splice variant of the GRB-IR cDNA such that
GRB10/IR-SV1 contains an intact pleckstrin homology domain and a
distinct amino terminus. The interaction of GRB10/IR-SV1 with the
insulin receptor and the insulin-like growth factor I (IGF-I) receptor
is mediated by the SH2 domain, and we show that glutathione
S-transferase-SH2 domain fusion proteins interact
specifically in vitro with the insulin receptor derived
from mammalian cells. The GRB10/IR-SV1 SH2 domain also interacted with
an ~135-kDa phosphoprotein from unstimulated cell lysates, an
interaction that decreased after insulin stimulation. We present
evidence that the GRB10/IR-SV1 protein plays a functional role in
insulin and IGF-I signaling by showing that microinjection of an SH2
domain fusion protein inhibited insulin- and IGF-I-stimulated
mitogenesis in fibroblasts, yet had no effect on mitogenesis
induced by epidermal growth factor. Our findings suggest that
GRB10/IR-SV1 may serve to positively link the insulin and IGF-I
receptors to an uncharacterized mitogenic signaling pathway.
Volume 271, Number 37,
Issue of September 13, 1996
pp. 22506-22513
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
EVIDENCE FOR A ROLE IN MITOGENIC SIGNALING
,
,
Department of Physiology, University of
Maryland School of Medicine, Baltimore, Maryland 21201 and the
§ Department of Medicine, University of California at San
Diego, La Jolla, California 92093
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T. J. O'Neill, Y. Zhu, and T. A. Gustafson Interaction of MAD2 with the Carboxyl Terminus of the Insulin Receptor but Not with the IGFIR. EVIDENCE FOR RELEASE FROM THE INSULIN RECEPTOR AFTER ACTIVATION J. Biol. Chem., April 11, 1997; 272(15): 10035 - 10040. [Abstract] [Full Text] [PDF]
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