IndraLab

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EGF phosphorylates PTK2. 10 / 63
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"Long et al. reported that a splicing isoform of SRC-3, SRC-3Δ4 can mediate Epidermal Growth Factor Receptor (EGFR) and Focal Adhesion Kinase (FAK) interaction, promoting EGF-induced FAK and c-Src phosphorylation and breast cancer cell migration ( xref )."
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"It was observed that expression of WT PKN1 increased TGFbeta1- and EGF dependent phosphorylation of FAK while KN PKN1 expression decreased this effect (XREF_FIG)."
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"Moreover, the results of this study showed that EGF induced FAK phosphorylation in Caco-2 cancer cells, and FAK inhibitors could inhibit EGF-induced FAK phosphorylation in colorectal cancer."
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"In this study, we observed that wild-type PTEN inhibited FAK phosphorylation stimulated by EGF, whereas phosphatase inactive mutant PTEN permitted the induction of FAK phosphorylation."
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"Thus, in rat pancreatic acini the phosphorylation of p125 FAK and paxillin by EGF depends on the integrity of the actin cytoskeleton."
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"EGF, HGF, and IGF-1 stimulate FAK phosphorylation in various cells."
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"Jeong et al. probed that melittin could constrain EGF-induced MMP-9 expression via blocking the NF- κ B and PI3K/Akt/mTOR signaling pathway and repress EGF-induced FAK phosphorylation through inhibiting the mTOR/p/0S6K/4E-BP1 signaling pathway in breast cancer cells [ xref ]."
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"Another finding of our study was the observation that CD73 enhanced invasion and metastasis of HNSCC cells, mediated by activation of EGF and EGFR signaling, and its downstream phosphorylation of FAK."
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"3.5 EBP50 increases EGF-dependent FAK phosphorylation."
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"Moreover, the rapid decrease in the EGF-stimulated p125 FAK and paxillin tyrosine phosphorylation contrasts with previous results showing a sustained increased in p125 FAK and paxillin tyrosine phos[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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EGF leads to the phosphorylation of PTK2 on tyrosine. 10 / 22
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"Our results support the conclusion that p21 rho is important for the ability of EGF to stimulate tyrosine phosphorylation in pancreatic acini because C3 transferase pretreatment markedly inhibited EGF[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Treatment of pancreatic acini with cytochalasin D completely inhibited tyrosine phosphorylation of p125 FAK, p130 Cas, and paxillin stimulated by CCK-8 and EGF in rat pancreatic acini [13,23,42]."
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"In the present study we found that cytochalasin D, which disrupts the integrity of the actin cytoskeleton [38], completely inhibited EGF stimulated p125 FAK and paxillin tyrosine phosphorylation in pa[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Two recent studies in other tissues [19,20] report that EGF can also stimulate tyrosine phosphorylation of p125 FAK and paxillin, suggesting it could be an important signaling cascade for the EGF rece[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Moreover, pretreatment of pancreatic acini with 100 muM LY294002 for 1 h caused a 49 +/-12% and 47 +/-14% decrease in the tyrosine phosphorylation of p125 FAK and paxillin by EGF (10 nM), respectively[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"To determine whether PKC activation might be involved in mediating the EGF stimulated changes in p125 FAK and paxillin tyrosine phosphorylation, we examined the effect of a PKC inhibitor, GF109203X [3[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Therefore, the fact that EGF stimulates PLCgamma activity raises the possibility that PKC activation or calcium mobilization could be possible mediators of EGF stimulation of p125 FAK and paxillin tyr[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In contrast, EGF or PDGF did not stimulate the tyrosine phosphorylation of FAK."
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"XREF_BIBR - XREF_BIBR Here, we stress our new finding in this experiment that EGF caused tyrosine phosphorylation of FAK (Y397) and p130cas (Y410), and Fn caused general phosphorylation of ERK, which were neglected before."
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"However, given that pY-β-PIX/FAK/paxillin in Src inhibitor-treated podocytes was blunted basally but remained partially responsive to EGF stimulation, it is likely that Src is not the sole regulator of the signaling pathway responsible for EGF-mediated tyrosine phosphorylation of β-PIX, FAK, and paxillin.Collectively, our findings support a model wherein CdGAP interacts with β-PIX in the cytoplasm and contributes to maintaining low Rac1/Cdc42 activity at basal conditions."
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EGF leads to the phosphorylation of PTK2 on S910. 10 / 12
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"In addition, the increase in the phosphorylation of FAK at Ser-910 induced by either LPA or EGF was abrogated by treatment with the MEK inhibitor U0126."
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"We found that either carbachol or EGF promoted a striking ERK-dependent phosphorylation of FAK at Ser-910, but only slight stimulation of FAK at Tyr-397 in these cells."
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"We found that either carbachol or EGF promoted a striking ERK-dependent phosphorylation of FAK at Ser-910, but these agonists caused only slight stimulation of FAK at Tyr-397 in T84 cells."
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"In order to determine whether EGF promotes FAK Ser-910 phosphorylation, cultures of IEC-18 cells were treated with EGF at 5 ng/ml for various times (1–60 min) and then FAK phosphorylation at Ser-910 w[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Stimulation with bombesin or the epidermal growth factor (EGF) induced phosphorylation of endogenous FAK at Ser-910 via an ERK-dependent pathway in Swiss 3T3 cells [29] ."
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"In addition, the increase in the phosphorylation of FAK at Ser 910 induced by either LPA or EGF was abrogated by treatment with the MEK inhibitor U0126."
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"These results indicate that EGF-induced FAK Ser-910 phosphorylation is mediated through an ERK-dependent pathway in IEC-18 cells."
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"Our results demonstrate, for the first time, that stimulation with bombesin, lysophosphatidic acid, PDB, or EGF induces phosphorylation of endogenous FAK at Ser-910 via an ERK-dependent pathway in Swiss 3T3 cells."
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"In order to examine whether EGF promotes FAK Ser-910 phosphorylation, monolayers of T84 cells, grown on permeable supports, were stimulated apically or basolaterally with 50 ng/ml EGF for 10 min."
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"Lysophosphatidic acid and epidermal growth factor (EGF) also stimulated FAK phosphorylation at Ser-910."
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EGF leads to the phosphorylation of PTK2 on Y925. 5 / 5
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"Phosphorylation of Tyr 925 of FAK in response to EGF was significantly reduced in KO cell compared to WT cells."
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"Of note, FAK phosphorylation at Y925 was also induced by activation of EGF-R tyrosine kinase by the proinvasive agent EGF [20] in both HCT8 and S11 and SW480 cells."
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"This phosphorylation of FAK on Y925 was also induced by the proinvasive agent EGF."
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"EGF activates c-Src and induces FAK phosphorylation on a functionally essential residue Y925; both events are critical for EGF induced cell migration."
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"As expected and similar to the effect of SRC-3Delta4 knockdown (XREF_FIG), expression of PAK1KD greatly decreased EGF stimulated FAK phosphorylation at Y925 (XREF_SUPPLEMENTARY)."
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EGF phosphorylates PTK2 on Y397. 3 / 3
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"CD99CRIII3 inhibited EGF-induced phosphorylation of FAK at Y397."
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"XREF_BIBR - XREF_BIBR Here, we stress our new finding in this experiment that EGF caused tyrosine phosphorylation of FAK (Y397) and p130cas (Y410), and Fn caused general phosphorylation of ERK, which were neglected before."
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"Integrin stimulated FAK autophosphorylation at Tyr 397 and epidermal growth factor (EGF)-stimulated trans-phosphorylation of FAK at Tyr 397 creates a high-affinity binding site for the Src-homology 2 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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EGF leads to the phosphorylation of PTK2 on A549. 1 / 1
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"Bee venom enhanced the upregulation of E-cadherin and the downregulation of vimentin and inhibited EGF-induced ERK, JNK, FAK, and mTOR phosphorylation in A549 cells."
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