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EGF phosphorylates STAT1. 24 / 24
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"In light of this result and the positive correlation found between EGFR and STAT1, we hypothesized that EGF may be activating STAT1 phosphorylation, mediated by JAK2."
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"The mecha- nism of STAT activation by receptor tyrosine kinases such as the epidermal growth factor (EGF), ptatelet derived growth factor (PDGF), and colony stimulating factor 1 (CSF1) receptors is le[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"EGF-induced phosphorylation of STAT1 was again completely blocked by our nuclear-localized EGFR inhibitor, a condition that has no effect on ERK1/2 phosphorylation (Fig.  xref )."
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"On the other hand, the ubiquitin RNAi did not inhibit the phosphorylation of STAT1 and ERK by IFN-gamma and EGF, respectively, suggesting that the silencing of ubiquitin expression under these experimental conditions did not have a general adverse effect on cell signaling (XREF_SUPPLEMENTARY)."
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"In light of this result and the positive correlation found between EGFR and STAT1, we hypothesized that EGF may be activating STAT1 phosphorylation, mediated by JAK2."
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"It has been shown that EGF induces STAT-1 phosphorylation, a known downstream target of this receptor ( xref )."
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"In contrast, pretreatment with trametinib drastically alters the STAT1:ERK1/2 activation ratio by completely preventing downstream phosphorylation of ERK1/2, while leading to a slight increase in EGF-induced phosphorylation of STAT1 (Fig.  xref )."
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"Additionally, inhibition of endosomal signaling using an EGFR inhibitor linked to a nuclear localization signal specifically prevents EGF-induced STAT1 phosphorylation and cell death, without affecting EGFR:ERK1/2 signaling."
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"On the other hand, the ubiquitin RNAi did not inhibit the phosphorylation of STAT1 and ERK by IFN-γ and EGF, respectively, suggesting that the silencing of ubiquitin expression under these experimental conditions did not have a general adverse effect on cell signaling ( xref )."
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"Indeed, EGF induced STAT1 (tyrosine701) phosphorylation reaching its maximum peak at 24 hours, while total STAT1 levels remained stable ( xref )."
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"The SH2 domain of Fyn bound to EGCG with a Kd value of 0.367 ± 0.122 μM. Based on these and other findings, the authors proposed that EGCG inhibits the EGF-induced transformation through inhibition of EGF-induced Fyn phosphorylation, which causes p38 MAPK activation and subsequent activation of STAT1, ATF-2, and AP-1 [27]."
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"Consistent with the notion that only endocytosed EGFR molecules have access to the nuclear pool of STAT1, pretreatment of NME-LM1 cells with this chimeric NLS-gefitinib molecule led to potent blockade of EGF-induced STAT1 phosphorylation without affecting phosphorylation of ERK1/2 (Fig.  xref )."
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"It has been shown that EGF induces STAT-1 phosphorylation, a known downstream target of this receptor."
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"We found that pharmacological inhibition of Syk could attenuate the EGF-induced phosphorylation of EGFR, JNK, p38 MAPK, STAT1, and STAT3 in A431, CAL27 and SAS cells."
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"The tyrosine kinase JAK1 and the transcription factors STAT1 and STAT3 are phosphorylated in response to epidermal growth factor (EGF) and other growth factors."
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"Accordingly, the EGFR-AA construct was not able to induce phosphorylation of STAT1 in response to EGF (Fig. 4b)."
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"EGF stimulation of Ca1a cells stably or transiently replenished with EGFR expression led to robust phosphorylation of EGFR and STAT1 and induction of apoptosis (Figs."
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"First, EGF promoted the tyrosine phosphorylation of STAT1 in IEC-6 cells and caused its translocation to the nucleus."
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"Although EGF and IFN-γ caused phosphorylation of Stat1 at both sites, only EGF activated p38 phosphorylation."
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"The tyrosine kinase JAK1 and the transcription factors STAT1 and STAT3 are phosphorylated in response to epidermal growth factor (EGF) and other growth factors."
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"The results demonstrated that EGF treatment increased the phosphorylation of EGFR, JAK1, JAK2, STAT1 and STAT3, increased the expression levels of cyclinD1 and cyclinE, promoted the cells to enter Sphase, and stimulated transcriptional activity in the cells."
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"Although EGF and IFN-gamma caused phosphorylation of Stat1 at both sites, only EGF activated p38 phosphorylation."
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"In A431 cells, a human epidermoid carcinoma cell line, that endogenously expresses high levels of epidermal growth factor receptor, it was shown that c-Src kinase activity was required for the epidermal growth factor-induced tyrosine phosphorylation of STAT1, STAT3, and STAT5 ( xref )."
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"However, EGF-induced tyrosine phosphorylation of STAT1 decreased only in 8a."
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