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JAK2 phosphorylates STAT3 on tyrosine. 34 / 34
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"Furthermore, our study reveals that PDGF-BB- and bFGF induced proliferation does not affect the osteogenic differentiation potential of hBMMSCs.All of the three GFs activated the hBMMSC ERK1/2 pathway[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Upon activation, STAT3 is phosphorylated by the non receptor protein tyrosine kinases janus kinase 2 (JAK2), leading to the formation of STAT3 dimer and translocation into the nucleus [XREF_BIBR, XREF_BIBR]."

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"Tyrphostin AG490, a specific inhibitor of Jak-2, significantly reduced tyrosine phosphorylation and DNA binding activity of STAT-3 and DNA synthesis induced by 5 (S)-HETE."

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"Additionally, Janus kinase 2 (JAK2) and tyrosine kinase 2 (TYK2) were recruited onto MyD88 to induce the phosphorylation and activation of the transcription factor signal transducer and activator of transcription-3 (STAT-3)."

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"The histamine induced enhancement of activity or tyrosine and serine phosphorylation of STAT3 were suppressed by pyrilamine, but not by cimetidine or thioperamide, which suggests the involvement of H1[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Upon cytokine stimulation, Janus kinase 2 (JAK2) phosphorylates STAT3 at tyrosine residues, which leads to the dimerization of STAT3 via reciprocal interactions between the SH2 domain of one monomer and the phosphorylated tyrosine of the other."

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"Binding of IL-5 to its specific receptor activates JAK2 which leads to the tyrosine phosphorylation of STAT3 proteins."

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"XREF_BIBR SD-1029 appears to act by inhibiting the kinase JAK2, which mediates STAT3 tyrosine phosphorylation in a range of tumor types."

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"WP1066 is a JAK-2 kinase inhibitor that blocks STAT3 tyrosine phosphorylation, and has proapoptotic and antiproliferative activity in a variety of cancers, including glioma [XREF_BIBR, XREF_BIBR]."

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"The stimulation of JAK2 activity then in turn enhances STAT1 and STAT3 Tyr phosphorylation and DNA binding activity, which identifies STAT transcription factors as downstream targets of CER."

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"JAK2 phosphorylates STAT3 on tyrosine leading to dimerization and nuclear localization, whereas MAPK phosphorylates STAT3 on serine 727, leading to maximal transcriptional activation of STAT3 [42]."

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"JAK2 inhibition prevented STAT3 tyrosine phosphorylation and NF-kappaB activation."

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"During this process, STAT3 was phosphorylated by the tyrosine kinase JAK2 that was recruited to the a7 subunit of the nicotinic acetylcholine [XREF_BIBR]."

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"Furthermore, PDGF-BB-induced STAT3 tyrosine and serine phosphorylation in hBMMSCs are directly mediated by JAK2 and ERK1/2, respectively."

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"Researchers found PPARgamma agonists blocked the cytokines induced tyrosine phosphorylation of STAT3 transcription factors and the upstream JAK2 in cells [27]."

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"Upon leptin binding and clustering of activated receptor complexes, Janus Kinase 2 (JAK2) phosphorylates intracellular tyrosine residues, which recruit transcription factors : Src Homology Phosphatase 2 (SHP2), Signal Transduscer and Activator of Transcription 5 (STAT5), and STAT3."

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"STAT3 was phosphorylated by the tyrosine kinase Jak2 that was recruited to the alpha7 subunit of the nicotinic acetylcholine receptor."

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"More specifically, CNTF activates JAK1, JAK2 and TYK2 tyrosine kinases which phosphorylate STAT3 tyrosine in position 705 [38-42]."

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"Specifically, we reveal that JAK2 mediates STAT3 tyrosine phosphorylation in response to the two BMPs, whereas BMP2- and BMP4 induced STAT3 serine phosphorylation involves two divergent cascades, namely the mTOR and ERK1/2 cascades, respectively."

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"These results suggest that JAK2 and ERK may mediate tyrosine and serine phosphorylation of STAT3 induced by histamine, respectively, and that both phosphorylations may be required for the activation o[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Once the gp130 receptor is activated, it induces downstream Janus kinase 2 (JAK2) phosphorylation of the tyrosine residue on STAT3."

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"IL-23 promotes signal transducer and transcriptional activator 3 (STAT3) phosphorylation by Janus kinase 2 (JAK2) and tyrosine kinase 2 (TYK2) by binding to its receptor IL-23R."

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"STAT3 phosphorylation by the tyrosine kinase Jak2 recruited to the alpha7nAChR is an underlying intracellular mechanism in this model."

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"Upon cytokine stimulation, Janus kinase 2 (JAK2) phosphorylates STAT3 at tyrosine residues, which leads to the dimerization of STAT3 via reciprocal interactions between the SH2 domain of one monomer and the phosphorylated tyrosine of the other."

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"STAT3 was phosphorylated by the tyrosine kinase Jak2, which is recruited to the alpha7 subunit of the nicotinic acetylcholine receptor."

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"JAK1 and JAK2 are known upstream kinases for tyrosine phosphorylation of STAT3, and overactivated in some types of cancer."

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"Dominant negative JAK1 or JAK2 was able to block the IGF-IR-mediated tyrosine phosphorylation of STAT3 in 293T cells."

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"Once the gp130 receptor is activated, it induces downstream Janus kinase 2 (JAK2) phosphorylation of the tyrosine residue on STAT3."

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"Tyrosine residue in STAT3 is phosphorylated by JAK or Src family kinases in response to cytokines or growth factors."

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"It was postulated that IL-23 promotes signal transducer and transcriptional activator 3 (STAT3) phosphorylation by Janus kinase 2 (JAK2) and tyrosine kinase 2 (TYK2) by binding to its receptor IL-23R (70, 71)."

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"32, 33 In the pathogenesis of cancer, elevated IL-6 and IL-27 could stimulate the activation of JAK1 and JAK2 enzymes, which subsequently mediate tyrosine phosphorylation of STAT3 at Tyr705."

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"In addition, JAK2 may directly tyrosine phosphorylate APRF, an ISGF like factor that rapidly migrates to the nucleus and binds to the hexanucleotide CTGGGA."

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"The second cascade would be a signaling pathway through PI3K, activated or not by JAK2, which could phosphorylate STAT3 via other non receptor tyrosine kinases like BMX XREF_BIBR."

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"On the other hand, both I/R and severe oxidative stress - but not moderate stress - increased tyrosine phosphorylation of STAT3 in an EGFR and JAK2-dependent manner."