The EGFR subfamily of receptor tyrosine kinases is composed of EGFR, ErbB2, ErbB3 and ErbB4. The EGFR shares 43%-44% aa sequence identity with the ECD of human EGFR subfamily. All these family members are type I transmembrane glycoproteins with an extracellular ligand binding domain. The extracellular ligand binding domain is containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a membrane-proximal tyrosine kinase domain. Ligand binding could induce EGFR homodimerization and heterodimerization with ErbB2, resulting in cell signaling, heterodimerization tyrosine phosphorylation and kinase activation. It can bind EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, HB-EGF, epigen, and so on. Its signaling regulates multiple biological functions including cell proliferation, differentiation, motility, and apoptosis. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR is overexpressed in different tumors. Several anti-cancer drugs use EGFR as target.
The EGFR subfamily of receptor tyrosine kinases is composed of EGFR; ErbB2; ErbB3 and ErbB4. The EGFR shares 43% - 44% aa sequence identity with the ECD of human EGFR subfamily. All these family members are type I transmembrane glycoproteins with an extracellular ligand binding domain. The extracellular ligand binding domain is containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a membrane-proximal tyrosine kinase domain. Ligand binding could induce EGFR homodimerization and heterodimerization with ErbB2; resulting in cell signaling; heterodimerization tyrosine phosphorylation and kinase activation. It can bind EGF; amphiregulin; TGF-alpha; betacellulin; epiregulin; HB-EGF; epigen; and so on. Its signaling regulates multiple biological functions including cell proliferation; differentiation; motility; and apoptosis. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR is overexpressed in different tumors. Several anti-cancer drugs use EGFR as target.
EGFR,also named as ERBB1,is a cell-surface receptor for members of the epidermal growth factor family (EGF-family) of extracellular protein ligands. Binding of the protein to a ligand induces receptor dimerization and tyrosine autophosphorylation and leads to cell proliferation. The gene resides on chromosome 7p12,encoding a 170 kDa membrane-associated glycoprotein. Recent studies have shown EGFR plays a critical role in cancer development and progression,including cell proliferation,apoptosis,angiogenesis,and metastatic spread. Mutations in this gene are associated with lung cancer.
EGR-1 belongs to the EGR family of C2H2-type zinc finger proteins. It is a nuclear protein and functions as a transcriptional regulator. EGR-1 recognizes and binds to the DNA sequence 5'-CGCCCCCGC-3'(EGR-site).The products of target genes it activates are required for differentiation and mitogenesis. Studies suggest this is a tumor suppressor gene. EGR-1 has a distinct pattern of expression in the brain, and its induction has been shown to be associated with neuronal activity. Several studies suggest it has a role in neuronal plasticity. EGR-1 has also been found to regulate the expression of synaptobrevin II (a protein important for synaptic exocytosis).
EG-VEGF, also known as prokineticin-1, is a member of the AVIT (prokineticin) family. Prokineticins are secreted proteins that can promote angiogenesis and induce strong gastrointestinal smooth muscle contraction. EG-VEGF can be detected in the steroidogenic glands, ovary, testis, adrenal and placenta. EG-VEGF has little or no effect on a variety of other endothelial and non-endothelial cell types. It induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. It directly influences neuroblastoma progression by promoting the proliferation and migration of neuroblastoma cells. EG-VEGF may play a role in placentation. It may also function in normal and pathological testis angiogenesis. It positively regulates PTGS2 expression and prostaglandin synthesis.
Eukaryotic Translation Initiation Factor 1A, X-Chromosomal (EIF1AX) is an essential eukaryotic translation initiation factor that belongs to the eIF-1A family. EIF1AX is required for the binding of the 43S complex (a 40S subunit, eIF2/GTP/Met-tRNAi and eIF3) to the 5' end of capped RNA and has been shown to interact with IPO13. EIF1AX contains one S1-like domain and seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.
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