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J Biol Chem. 1997 Mar 28;272(13):8121-4.

SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes.

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  • 1Center for Neurological Disease, Brigham and Women's Hospital and Department of Neurology, Harvard Medical School, Boston, Massachusetts 02114, USA.


Based on the presence of multiple proline-rich motifs in the huntingtin sequence, we tested its possible association with epidermal growth factor (EGF) receptor signaling complexes through SH3 domain-containing modules. We found that huntingtin is associated with Grb2, RasGAP, and tyrosine-phosphorylated EGF receptor. These associations are regulated by activation of the EGF receptor, suggesting that they may be part of EGF receptor-mediated cellular signaling cascade. In vitro binding studies indicate that SH3 domains of Grb2 or RasGAP are required for their binding to huntingtin. Our results suggest that huntingtin may be a unique adapter protein for EGF receptor-mediated signaling and may be involved in the regulation of Ras-dependent signaling pathways.

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