共查询到20条相似文献,搜索用时 31 毫秒
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Stress-induced phosphorylation of STAT1 at Ser727 requires p38 mitogen-activated protein kinase whereas IFN-gamma uses a different signaling pathway 总被引:4,自引:0,他引:4 下载免费PDF全文
Kovarik P Stoiber D Eyers PA Menghini R Neininger A Gaestel M Cohen P Decker T 《Proceedings of the National Academy of Sciences of the United States of America》1999,96(24):13956-13961
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Collaboration of signal transducer and activator of transcription 1 (STAT1) and BRCA1 in differential regulation of IFN-gamma target genes 总被引:15,自引:0,他引:15 下载免费PDF全文
Ouchi T Lee SW Ouchi M Aaronson SA Horvath CM 《Proceedings of the National Academy of Sciences of the United States of America》2000,97(10):5208-5213
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Wilbanks AM Mahajan S Frank DA Druker BJ Gilliland DG Carroll M 《Experimental hematology》2000,28(5):584-593
OBJECTIVE: TEL/PDGFbetaR is a tyrosine kinase fusion protein associated with the pathogenesis of chronic myelomonocytic leukemia. The following experiments were undertaken to understand the mechanisms whereby TEL/PDGFbetaR transforms cells. MATERIALS AND METHODS: Activation of JAK and STAT proteins was studied in an interleukin 3 (IL-3)-dependent cell line, Ba/F3, transformed to IL-3 independence by TEL/PDGFbetaR. RESULTS: TEL/PDGFbetaR activates STAT1 and STAT5 in transformed Ba/F3 cells through a JAK-independent pathway. Activation of STAT proteins requires the kinase activity of TEL/PDGFbetaR. JAK1, JAK2, JAK3, and TYK2 are not phosphorylated by TEL/PDGFbetaR. However, TEL/PDGFbetaR can phosphorylate STAT5 in transiently transfected COS cells, suggesting that TEL/PDGFbetaR may itself be the kinase involved in tyrosine phosphorylation of STAT proteins. In contrast, native PDGFbetaR stimulated by PDGF ligand does not activate STAT proteins to a significant degree in this hematopoietic context. STAT1 and STAT5 also are activated by TEL/ABL and TEL/JAK2 fusion proteins associated with human leukemia. CONCLUSIONS: STAT activation may be a common mechanism of transformation by leukemogenic tyrosine kinase fusion proteins. 相似文献
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Mechanical stretch activates the JAK/STAT pathway in rat cardiomyocytes. 总被引:15,自引:0,他引:15
J Pan K Fukuda M Saito J Matsuzaki H Kodama M Sano T Takahashi T Kato S Ogawa 《Circulation research》1999,84(10):1127-1136
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Experiments were performed to define the basis for negative regulation of STAT3 activation (i.e., Tyr705 phosphorylation) by angiotensin II in cardiomyocytes. Treatment of cardiomyocytes with angiotensin II resulted in rapid and sustained phosphorylation of STAT3 on Ser727; in contrast, STAT3 Tyr705 phosphorylation was decreased, with dephosphorylation being most pronounced at 30 minutes. Angiotensin II-induced STAT3 Tyr705 dephosphorylation was not prevented by inhibiting protein synthesis, but was blocked by vanadate or the MEK inhibitor PD98059. PD98059 was found to inhibit angiotensin II-induced Erk activation and STAT3 Ser727 phosphorylation. Angiotensin II also attenuated LIF-induced STAT3 Tyr705 phosphorylation, and this effect could be blocked with PD89059. These results are consistent with Erk-mediated STAT3 Ser727 phosphorylation leading to STAT3 Tyr705 dephosphorylation, and accounting for angiotensin II-mediated STAT3 inhibition in cardiomyocytes. We propose that Erk serves as a scaffolding protein in recruiting either a protein tyrosine or MAP kinase phosphatase to STAT3. 相似文献
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Interleukin 12 induces tyrosine phosphorylation and activation of STAT4 in human lymphocytes. 总被引:24,自引:0,他引:24 下载免费PDF全文
C M Bacon E F Petricoin rd J R Ortaldo R C Rees A C Larner J A Johnston J J O'Shea 《Proceedings of the National Academy of Sciences of the United States of America》1995,92(16):7307-7311
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Yang J Huang J Dasgupta M Sears N Miyagi M Wang B Chance MR Chen X Du Y Wang Y An L Wang Q Lu T Zhang X Wang Z Stark GR 《Proceedings of the National Academy of Sciences of the United States of America》2010,107(50):21499-21504
Following its tyrosine phosphorylation, STAT3 is methylated on K140 by the histone methyl transferase SET9 and demethylated by LSD1 when it is bound to a subset of the promoters that it activates. Methylation of K140 is a negative regulatory event, because its blockade greatly increases the steady-state amount of activated STAT3 and the expression of many (i.e., SOCS3) but not all (i.e., CD14) STAT3 target genes. Biological relevance is shown by the observation that overexpression of SOCS3 when K140 cannot be methylated blocks the ability of cells to activate STAT3 in response to IL-6. K140 methylation does not occur with mutants of STAT3 that do not enter nuclei or bind to DNA. Following treatment with IL-6, events at the SOCS3 promoter occur in an ordered sequence, as shown by chromatin immunoprecipitations. Y705-phosphoryl-STAT3 binds first and S727 is then phosphorylated, followed by the coincident binding of SET9 and dimethylation of K140, and lastly by the binding of LSD1. We conclude that the lysine methylation of promoter-bound STAT3 leads to biologically important down-regulation of the dependent responses and that SET9, which is known to help provide an activating methylation mark to H3K4, is recruited to the newly activated SOCS3 promoter by STAT3. 相似文献
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Tyrosine phosphorylation and activation of STAT5, STAT3, and Janus kinases by interleukins 2 and 15. 总被引:22,自引:0,他引:22 下载免费PDF全文
J A Johnston C M Bacon D S Finbloom R C Rees D Kaplan K Shibuya J R Ortaldo S Gupta Y Q Chen J D Giri et al. 《Proceedings of the National Academy of Sciences of the United States of America》1995,92(19):8705-8709