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

http://www.ncbi.nlm.nih.gov/pubmed/9079622

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.

Pubmed ID: 9079622 RIS Download

Mesh terms: Adaptor Proteins, Signal Transducing | GRB2 Adaptor Protein | GTPase-Activating Proteins | Humans | Huntington Disease | Macromolecular Substances | Nerve Tissue Proteins | Nuclear Proteins | Proteins | Receptor Protein-Tyrosine Kinases | Receptor, Epidermal Growth Factor | Signal Transduction | Tumor Cells, Cultured | ras GTPase-Activating Proteins | src Homology Domains

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