MinireviewIdentification of functional domains in the hepatocyte growth factor and its receptor by molecular engineering
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Cited by (43)
The hepatocyte growth factor isoform NK2 activates motogenesis and survival but not proliferation due to lack of Akt activation
2016, Cellular SignallingCitation Excerpt :Upon binding to the receptor, HGF induces activation of Met by auto-phosphorylation of a several critical tyrosine residues: juxtamembrane Y1003 that is responsible for Met endocytic processing and degradation [21,22]; Y1234 and Y1235 in the kinase domain that are required for kinase activity of the receptor [23]; and Y1349 and Y1356 in the multisubstrate docking domain that are responsible for recruitment of multiple adaptor proteins upon phosphorylation [24]. Depending on the proteins recruited to the receptor in a specific cell type, Met activates a variety of signaling cascades, including Ras/p42/p44 mitogen activated protein kinase (MAPK), phosphatidylinositol 3-kinase (PI3K)/AKT, signal transducer and activator of transcription 3 (STAT3), src homology phosphatase 2 (SHP2), phospholipase C-gamma (PLC-γ), src kinase, protein kinase C (PKC) isoforms, and/or small GTP-binding proteins Rap1, Rac, and Rho [25–36]. The identification of individual signaling pathways required for the specific biological activities of HGF is complicated and appears to have substantial overlap [32,33,37–40].
The hepatocyte growth factor (HGF)-MET receptor tyrosine kinase signaling pathway: Diverse roles in modulating immune cell functions
2016, CytokineCitation Excerpt :The extracellular domain contains a SEMA (characteristic of semaphorins) domain, a PSI (present in plexins, semaphorins and integrins) domain and four IPT (immunoglobulin-like fold shared by plexins and transcription factors) domains. During biosynthetic transport, MET is cleaved within the SEMA domain by intracellular endoproteases to generate a 50 kDa α chain that is completely extracellular in location and a 145 kDa β chain, which contains the rest of the precursor protein [51–53]. Uncleaved MET retains the capacity to bind ligand and can transduce signals [54].
Opportunities and Challenges in Tumor Angiogenesis Research. Back and Forth Between Bench and Bed
2012, Advances in Cancer ResearchCitation Excerpt :Ang-2 is strongly expressed in the vasculature of many tumors, suggesting that Ang-2 may act synergistically with other cytokines such as VEGF to promote tumor-associated angiogenesis and tumor progression (Hu and Cheng, 2009). The intracellular portion is responsible for signal transduction; it contains a juxtamembrane domain, a tyrosine kinase domain, and a C-terminal regulatory tail (Bardelli et al., 1994). In the juxtamembrane domain, phosphorylation of Ser 985 can downregulate the tyrosine kinase activity (Gandino et al., 1994), while phosphorylation of Tyr 1003 can induce polyubiquitination and degradation of c-Met (Peschard et al., 2004).
Role of c-Met in Cancer: Emphasis on Lung Cancer
2009, Seminars in Oncology