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GRB2 binds EGFR and SH2 domain. 7 / 7
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"For example, Grb2 directly binds EGFR and Ras via its SH2 domain, while the SH2 domain of Nck binds PDGFR and ephrinb1 receptors among others (Bong et al., 2004; Cowan and Henkemeyer, 2018; Lettau et al., 2009; Nishimura et al., 1993; Pramatarova et al., 2003)."
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"The SH2 domain of GRB2 binds to the tyrosine auto- phosphorylation sites of activated EGF receptor [14], suggesting that the interaction of Sem-5 with Let-23 is direct."
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"These discoveries were extended to mammalian systems, where it was shown that the Grb2 SH2 domain could inducibly bind the tyrosine phosphorylated epidermal growth factor receptor (EGFR) while bound constitutively to son of sevenless (SOS), a guanine nucleotide exchange factor for Ras."
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"In fact, CBL binding—and subsequent ubiquitination—relies on the cooperative binding of EGFR through direct interactions between phosphotyrosines on the EGFR C-terminal tail and an SH2-like domain on CBL, as well as via the adapter growth factor receptor bound protein 2 (GRB2), which itself binds phosphotyrosines on EGFR via its SH2 domain ."
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"The Grb2/Sos complex binds to the activated EGFR through the SH2 domain of Grb2, recruiting Sos to the plasma membrane where the Ras protein is located."
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"Grb2 binds to the tyrosine phosphorylated cytoplasmic tail of the activated epidermal growth factor receptor through its SH2 domain and thereby relocates Sos from the cytoplasm to the plasma membrane [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"GRB2 binds the EGFR and contains one SH2 domain and two SH3 domains, which are crucial for IL3 signaling in hematopoietic stem and progenitor cell."
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