ArticleProceedings of the National Academy of Sciences of the United States of America2003
Role of extracellular subdomains of p185c-neu and the epidermal growth factor receptor in ligand-independent association and transactivation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 24 citations in OpenAlex.
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- NK3R Mediates the EGF-Induced SLα Secretion and mRNA Expression in Grass Carp Pituitary.International journal of molecular sciences · 2018Article
- A monoclonal antibody targeting ErbB2 domain III inhibits ErbB2 signaling and suppresses the growth of ErbB2-overexpressing breast tumors.Oncogenesis · 2016Article
- Novel Peptidomimetics for Inhibition of HER2:HER3 Heterodimerization in HER2-Positive Breast Cancer.Chemical biology & drug design · 2015Article
- Design, synthesis and characterization of peptidomimetic conjugate of BODIPY targeting HER2 protein extracellular domain.European journal of medicinal chemistry · 2013Article
- Inhibition of protein-protein interaction of HER2-EGFR and HER2-HER3 by a rationally designed peptidomimetic.Journal of biomolecular structure & dynamics · 2012Article
- A conformationally constrained peptidomimetic binds to the extracellular region of HER2 protein.Journal of biomolecular structure & dynamics · 2010Article
- Mechanistic and signaling analysis of Muc4-ErbB2 signaling module: new insights into the mechanism of ligand-independent ErbB2 activity.Journal of cellular physiology · 2010Article
- Estrogen receptor-alpha mediates the epidermal growth factor-stimulated prolactin expression and release in lactotrophs.Endocrinology · 2009Article
- Molecular modeling of nearly full-length ErbB2 receptor.Biophysical journal · 2005Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We investigated the assembly and activation of the epidermal growth factor receptor (EGFR)-p185c-neu heterodimer by using a sequential immunoprecipitation methodology. Using this approach we detected heterodimers and also higher-ordered oligomeric complexes. Phosphorylated EGFR-p185c-neu heterodimeric forms were detected in the absence of EGF, but the species became highly phosphorylated after EGF stimulation. To evaluate heterodimer formation and additional transactivation by EGF, we investigated the roles of the four extracellular subdomains of p185c-neu and the EGFR. Subdomains I-IV of the EGFR dimerized with subdomains I-IV of p185c-neu, respectively, in a parallel manner. In addition, subdomains I-IV of the EGFR also associated with p185c-neu subdomains III, IV, I, and II, respectively. A lack of one of the p185c-neu cysteine-rich domains (subdomains II or IV) resulted in a loss of EGF-induced transactivation. These data suggest that two cysteine-rich domains play defining roles in ligand-dependent transactivation and that both of these cysteine-rich extracellular subdomains as well as non-cysteine-rich extracellular subdomains are involved in ligand-independent interactions with the EGFR. Our studies provide biochemical evidence of the role of the cysteine-rich domains of p185c-neu in assembly and transactivation of erbB complexes and also indicate that these subdomains might be useful clinical targets.
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