![]() This regulation affects the SHC-Ras-ERK pathway. SHC proteins are differentially regulated by the Multiple Copies in T-cell malignancy(MCT-1). SHC1 is not a static scaffold protein, a protein that does not move or change over time, it is dynamic as the conformation changes and modifies the EGFR signaling output over time. PTPN122 then acts as a switch to convert SHC1 to SgK269-mediated pathways that regulate cell invasion and morphogenesis. This activation is followed by a sub-network of proteins that bind to SHC1 and are involved cytoskeleton reorganization, trafficking and signal termination. After the EGF stimulation SHC1 binds to groups of proteins that activate survival pathways. Activated tyrosine kinase receptors, on the cell surface, use proteins such as SHC1 that contain phosphotyrosine binding domains. SHC1 has been found to act in signaling information after epidermal growth factor (EGF) stimulation. P52SHC and p66SHC have been found in steroid hormone-regulated cancer and metastasizes. p66SHC functionally is also involved in regulating oxidative and stress- induced apoptosis – mediating steroid action through the redox signaling pathway. A rise in p66SHC promotes stress induced apoptosis. p66SHC inhibits ERK1/2 activity and antagonize mitogenic and survival abilities of T-lymphoma Jurkat cell lines. p52SHC and p46SHC activate the Ras-ERK pathway. The SHC and its adaptor proteins transmit signaling of the cell surface receptors such as EGFR, erbV-2 and insulin receptors. Overexpression of SHC proteins are associated with cancer mitogenesis, carcinogenesis and metastasis. P66SHC is characterized by having an additional N-terminal CH2 domain. Both of the domains for the three proteins can bind to tyrosine-phosphorylated proteins but they are different in their phosphopeptide-binding specificities. All three SHC1 proteins share the same domain arrangement consisting of an N-terminal phosphotyrosine-binding(PTB) domain and a C-terminal Src-homology2(SH2) domain. The three proteins that SHC1 codes for have distinctly different molecular weights. The protein SHC1 also acts as a scaffold protein which is used in cell surface receptors. These proteins differ in activity and subcellular locations, p66 is the longest and while the p52 and p46 link activated receptor tyrosine kinase to the RAS pathway. The gene SHC1 is located on chromosome 1 and encodes 3 main protein isoforms: p66SHC, p52SHC and p46SHC. SCOP classifies the 3D structure as belonging to the SH2 domain family. SHC has been found to be important in the regulation of apoptosis and drug resistance in mammalian cells. SHC-transforming protein 1 is a protein that in humans is encoded by the SHC1 gene. positive regulation of Ras protein signal transduction.positive regulation of cell population proliferation.regulation of superoxide metabolic process.positive regulation of cell proliferation in bone marrow.interleukin-2-mediated signaling pathway.interleukin-15-mediated signaling pathway.positive regulation of ERK1 and ERK2 cascade.positive regulation of transcription, DNA-templated.negative regulation of transcription, DNA-templated.negative regulation of apoptotic process.regulation of epidermal growth factor-activated receptor activity.regulation of cell population proliferation.IRE1-mediated unfolded protein response.cellular response to growth factor stimulus.epidermal growth factor receptor signaling pathway.
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