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PAG1 conferred inherent radioresistance by activating STAT3.
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Low PAG1 expression is associated neuroblastoma.
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Our study highlights the underlying mechanism of cross interaction between ASCs and breast cancer cells, and indicates that PAG1/Cbp in breast cancer cell may modulate tumor progression and acquired chemoresistance in the ASCs-associated breast cancer microenvironment through Src and AKT/mTOR pathways.
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Up-regulated expression of CBP in Jurkat cells could reduce cell homogeneity and promote cell apoptosis
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No association Pag1 mutation with patient with Schizophrenia.
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The risk-associated allele of rs2370615 predisposes to allergic disease by increasing PAG1 expression, which might promote B cell activation and have a pro-inflammatory effect.
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CBP may decrease the metastasis of esophageal carcinoma by inhibiting the activation of Src.
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The inhibitory function of novobiocin in disrupting the HIF1alpha/p300 complex might be important in tumor cell growth.
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siRNA directed against PAG1 in a radioresistant (Hep-2max) cell line dramatically enhanced the radiosensitivity and IR-induced cell death.
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expression of CBP gene is decreased in esophageal carcinoma, which might contribute to the tumorigenesis and progression.
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findings support a negative regulatory function for Cbp/PAG in proximal B cell receptor signaling in normal and EBV-transformed B cells
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An over-expression of PAG1 in PC-3M-1E8 cells effectively suppresses the activation of Ras and ERK, as well as the cyclin D1 expression, leading to an inhibition of the proliferation ability of tumor cells.
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Cbp down-regulation is primarily mediated by epigenetic histone modifications via oncogenic MAPK/PI3K pathways in a subset of cancer cells.
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Results indicate that Cbp is required for the Csk-mediated inactivation of c-Src and may control the promotion of malignancy in NSCLC tumors that are characterized by c-Src upregulation.
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PAG1 protein was downregulated in PC-3M-1E8 prostate cancer cell line.
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In the membrane environment of ALK+ lymphoma rafts, where the glycosphingolipid to signaling protein ratio is higher than in B-NHL rafts, the Lyn activity is suboptimal and does not allow the formation of an efficient Lyn-Cbp/PAG signalosome
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Study shows EGF-stimulation-induced Csk-binding protein (Cbp) tyrosine phosphorylation followed by Cbp-Csk association, in a SFK-dependent manner.
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High PAG-binding ability with CSK in vitro as well as the human PAG structure characterized by 11 alpha-helix structures including a 3 kDa transmembrane domain are reported.
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PAG negatively regulates Ras proteins, and by knocking down PAG there is enhanced Src kinase activity and Ras activation.
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engagement of the SH2 domain on PAG renders FynT insensitive to Csk negative regulation