SH2 domains prevent tyrosine dephosphorylation of the EGF receptor: identification of Tyr992 as the high-affinity binding site for SH2 domains of phospholipase C gamma.

Eitemau Tebyg

• Mutations in the cytoplasmic domain of EGF receptor affect EGF binding and receptor internalization.
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  Cyhoeddwyd: (1986)
• A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1.
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• The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors.
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• SH2 domains serve as lipid binding modules for pTyr-signaling proteins
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  Cyhoeddwyd: (2016)
• SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange.
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  Cyhoeddwyd: (1993)