Stress-induced interaction between p38 MAPK and HSP70
Stress-induced interaction between p38 MAPK and HSP70
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应激诱导的 p38 MAPK 和 HSP70 之间的相互作用
DOI：
10.1016/j.bbrc.2012.07.096
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发表时间：
2012-08-24
影响因子：
3.1
通讯作者：
Jiang, Yong
中科院分区：
文献类型：
--
作者：
Gong, Xiaowei;Luo, Tingting;Jiang, Yong
p38 MAPK是哺乳动物细胞中四个MAPK亚家族之一，可被环境应激和促炎细胞因子激活，在许多生物过程中发挥重要作用。尽管对p38的结构和功能已经有了很多了解，但仍然存在许多问题。活化和核易位的耦合是p38信号传导的一个重要方面。为了探索p38易位的潜在伴侣，我们进行了内源性下拉实验，并确定HSP70是p38的潜在相互作用蛋白。我们在体外和体内证实了p38和HSP70之间的相互作用，并确定了它们的相互作用域。我们还发现应力诱导这两种蛋白的核共定位。我们的初步结果表明，HSP70与p38特异性核下游靶点MK2的磷酸化有关，提示HSP70可能是p38核易位的潜在伴侣。(c) 2012 Elsevier Inc.版权所有。
p38 MAPK, one of the four MAPK subfamilies in mammalian cells, is activated by environmental stresses and pro-inflammatory cytokines, playing fundamental roles in many biological processes. Despite all that is known on the structure and functions of p38, many questions still exist. The coupling of activation and nuclear translocation represents an important aspect of p38 signaling. In our effort in exploring the potential chaperone for p38 translocation, we performed an endogenous pull-down assay and identified HSP70 as a potential interacting protein of p38. We confirmed the interaction, between p38 and HSP70 in vitro and in vivo, and identified their interaction domains. We also showed stress-induced nuclear co-localization of these two proteins. Our preliminary result indicated that HSP70 was related to the phosphorylation of MK2, a specific nuclear downstream target of p38, suggesting HSP70 is a potential chaperone for the nuclear translocation of p38. (c) 2012 Elsevier Inc. All rights reserved.