Mapk-activated protein kinase-2 (mk2)-mediated formation and phosphorylation-regulated dissociation of the signal complex consisting of p38, mk2, akt, and hsp27
文献类型：期刊论文
| 作者 | Zheng, Chunlei; Lin, Ziyang; Zhao, Zhizhuang Joe; Yang, Yajun; Niu, Hanben; Shen, Xun |
| 刊名 | Journal of biological chemistry
 |
| 出版日期 | 2006-12-01 |
| 卷号 | 281期号:48页码:37215-37226 |
| ISSN号 | 0021-9258 |
| DOI | 10.1074/jbc.m603622200 |
| 通讯作者 | Shen, xun(shenxun@sun5.ibp.ac.cn) |
| 英文摘要 | The p38 mapk and heat shock protein 27 (hsp27) form a signaling complex with serine/threonine kinase akt and mapk-activated protein kinase-2 (mk2), which plays an important role in controlling stress-induced apoptosis and reorganizing actin cytoskeleton. however, regulation of the complex is poorly understood. in this study, the interaction between p38 and hsp27 was visualized in single living l929 cells using fluorescence resonance energy transfer technology, while their association with akt was examined by immunoprecipitation analysis. under normal growth conditions, p38 kinase constitutively interacts with hsp27. when cells were exposed to h2o2 or stimulated by arachidonic acid, this interaction was disrupted. however, inhibition of the activation of p38 and akt by selective inhibitors or overexpression of the kinase-dead mutant of p38 diminished such effects. furthermore, mutation of phosphorylation sites of hsp27 renders the interaction resistant to h2o2 and arachidonic acid. it was interesting to find that the interaction disappeared in the cells from mk2-knock-out mice or the cells treated with lemptomycin b that blocks export of mk2 from nucleus to cytosol. however, mk2 is not required for the association of hsp27 with akt. this study suggests that mk2 mediates the incorporation of p38 into the pre-existing complex of hsp27 with akt. phosphorylation of hsp27 finally breaks the signaling complex. |
| WOS关键词 | HEAT-SHOCK-PROTEIN ; INDUCED TNF-ALPHA ; NUCLEAR EXPORT ; PHOSPHATIDYLINOSITOL 3-KINASE ; DOCKING INTERACTIONS ; ENDOTHELIAL-CELLS ; HUMAN NEUTROPHILS ; OXIDATIVE STRESS ; GROWTH-FACTOR ; LEPTOMYCIN B |
| WOS研究方向 | Biochemistry & Molecular Biology |
| WOS类目 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000242220800082 |
| 出版者 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2378890 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Shen, Xun |
| 作者单位 | 1.Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100101, Peoples R China 3.Shenzhen Univ, Minist Educ, Key Lab Opto Elect Devices & Syst, Shenzhen 518060, Peoples R China 4.Univ Oklahoma, Hlth Sci Ctr, Dept Pathol, Oklahoma City, OK 73104 USA |
| 推荐引用方式 GB/T 7714 | Zheng, Chunlei,Lin, Ziyang,Zhao, Zhizhuang Joe,et al. Mapk-activated protein kinase-2 (mk2)-mediated formation and phosphorylation-regulated dissociation of the signal complex consisting of p38, mk2, akt, and hsp27[J]. Journal of biological chemistry,2006,281(48):37215-37226. |
| APA | Zheng, Chunlei,Lin, Ziyang,Zhao, Zhizhuang Joe,Yang, Yajun,Niu, Hanben,&Shen, Xun.(2006).Mapk-activated protein kinase-2 (mk2)-mediated formation and phosphorylation-regulated dissociation of the signal complex consisting of p38, mk2, akt, and hsp27.Journal of biological chemistry,281(48),37215-37226. |
| MLA | Zheng, Chunlei,et al."Mapk-activated protein kinase-2 (mk2)-mediated formation and phosphorylation-regulated dissociation of the signal complex consisting of p38, mk2, akt, and hsp27".Journal of biological chemistry 281.48(2006):37215-37226. |
入库方式： iSwitch采集
来源：中国科学院大学
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。