• Register
X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

X

Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.

No
Yes

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

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

Authors

  • Liu YF
  • Deth RC
  • Devys D

Journal

The Journal of biological chemistry

Publication Data

March 28, 1997

Associated Grants

None

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