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Regulation of Stat3 activation by MEK kinase 1 总被引:6,自引:0,他引:6
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Bhattacharjee A Xu B Frank DA Feldman GM Cathcart MK 《Journal of immunology (Baltimore, Md. : 1950)》2006,177(6):3771-3781
Our previous studies demonstrated that the IL-13-induced 15-lipoxygenase expression in primary human monocytes is regulated by the activation of both Stat1 and Stat3 and by protein kinase C (PKC)delta. IL-13 stimulated the phosphorylation of Stat3 on both Tyr705 and Ser727. In this study we show that IL-13 induces the association of PKCdelta with Stat3, not with Stat1, and is required for Stat3 Ser727 phosphorylation. We found a novel IL-13-dependent cytosolic signaling complex of PKCdelta and tyrosine-phosphorylated Stat3. A tyrosine kinase inhibitor blocked PKCdelta association with Stat3 as well as Stat3 Ser727 phosphorylation. We therefore hypothesized that tyrosine phosphorylation was required for Stat3 interaction with PKCdelta and subsequent PKCdelta-dependent phosphorylation of Stat3 Ser727. We developed an efficient transfection protocol for human monocytes. Expression of Stat3 containing a mutation in Tyr705 inhibited the association of PKCdelta with Stat3 and blocked Stat3 Ser727 phosphorylation, whereas transfection with wild-type Stat3 did not. Furthermore, by transfecting monocytes with Stat3 containing mutations in Tyr705 or Ser727 or with wild-type Stat3, we demonstrated that both Stat3 tyrosine and serine phosphorylations are required for optimal binding of Stat3 with DNA and maximal expression of 15-lipoxygenase, an important regulator of inflammation and apoptosis. 相似文献
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Requirement for Ras/Rac1-mediated p38 and c-Jun N-terminal kinase signaling in Stat3 transcriptional activity induced by the Src oncoprotein. 总被引:9,自引:0,他引:9
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James Turkson Tammy Bowman Jalila Adnane Yi Zhang Julie Y. Djeu Madhavi Sekharam David A. Frank Lawrence B. Holzman Jie Wu Said Sebti Richard Jove 《Molecular and cellular biology》1999,19(11):7519-7528
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Progestins induce transcriptional activation of signal transducer and activator of transcription 3 (Stat3) via a Jak- and Src-dependent mechanism in breast cancer cells
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Proietti C Salatino M Rosemblit C Carnevale R Pecci A Kornblihtt AR Molinolo AA Frahm I Charreau EH Schillaci R Elizalde PV 《Molecular and cellular biology》2005,25(12):4826-4840
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