描述：
The EGF R subfamily of receptor tyrosine kinases comprises four members: EGF R (also
known as HER-1, ErbB1, or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4).
All family members are type I transmembrane glycoproteins. They contain an extracellular
ligand binding domain containing two cysteinerich domains and a cytoplasmic domain
containing a membraneproximal tyrosine kinase domain followed by multiple tyrosine
autophosphorylation sites. The mouse EGF R cDNA encodes a 1210 amino acid (aa) precursor
with a 24 aa signal peptide, a 623 aa extracellular domain (ECD), a 23 aa transmembrane
segment, and a 540 aa cytoplasmic domain. Soluble receptors consisting of the extracellular
ligand binding domain are generated by alternate splicing in human and mouse. Within the
ECD, mouse EGF R shares 88% and 93% aa sequence identity with human and rat EGF R,
respectively. It shares 44% 48% aa sequence identity with the ECD of mouse ErbB2, ErbB3,
and ErbB4. EGF R binds a subset of the EGF family ligands, including EGF, amphiregulin, TGF-α,
betacellulin, epiregulin, HB-EGF, and epigen. Ligand binding induces EGF R homodimerization
as well as heterodimerization with ErbB2, resulting in kinase activation, heterodimerization
tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers
with the ligandactivated ErbB3 or ErbB4. EGF R signaling regulates multiple biological functions
including cell proliferation, differentiation, motility, and apoptosis. EGF R is over-expressed in
a wide variety of tumors and is the target of several anticancer drugs.
原厂资料：
The EGF R subfamily of receptor tyrosine kinases comprises four members: EGF R (also
known as HER-1, ErbB1, or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4).
All family members are type I transmembrane glycoproteins. They contain an extracellular
ligand binding domain containing two cysteinerich domains and a cytoplasmic domain
containing a membraneproximal tyrosine kinase domain followed by multiple tyrosine
autophosphorylation sites. The mouse EGF R cDNA encodes a 1210 amino acid (aa) precursor
with a 24 aa signal peptide, a 623 aa extracellular domain (ECD), a 23 aa transmembrane
segment, and a 540 aa cytoplasmic domain. Soluble receptors consisting of the extracellular
ligand binding domain are generated by alternate splicing in human and mouse. Within the
ECD, mouse EGF R shares 88% and 93% aa sequence identity with human and rat EGF R,
respectively. It shares 44% 48% aa sequence identity with the ECD of mouse ErbB2, ErbB3,
and ErbB4. EGF R binds a subset of the EGF family ligands, including EGF, amphiregulin, TGF-α,
betacellulin, epiregulin, HB-EGF, and epigen. Ligand binding induces EGF R homodimerization
as well as heterodimerization with ErbB2, resulting in kinase activation, heterodimerization
tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers
with the ligandactivated ErbB3 or ErbB4. EGF R signaling regulates multiple biological functions
including cell proliferation, differentiation, motility, and apoptosis. EGF R is over-expressed in
a wide variety of tumors and is the target of several anticancer drugs.
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