Phospho-EGFR (Tyr1068) is the phosphorylated form of the epidermal growth factor receptor (EGFR) at the tyrosine residue 1068, indicating the activated state of EGFR. Upon binding of EGFR to its ligands (e.g., EGF), the receptor dimerizes and undergoes autophosphorylation, with phosphorylation at Tyr1068 being one of the key activation events. This modification provides a binding site for downstream signaling molecules (e.g., Grb2 and PI3K), thereby initiating signaling pathways such as MAPK/ERK and PI3K/AKT, which regulate cell proliferation, survival, migration, and differentiation. Abnormal phosphorylation at Tyr1068 is closely associated with the development, progression, and treatment resistance of various cancers (e.g., non-small cell lung cancer, colorectal cancer), making it an important biomarker for cancer diagnosis and targeted therapy.
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