Stress-induced interaction between p38 MAPK and HSP70
- Department of Pathophysiology and Key Laboratory of Proteomics of Guangdong Province, Southern Medical University, Guangzhou 510515 (China)
- Department of Pathology, Zhujiang Hospital, Southern Medical University, Guangzhou 510282 (China)
- Department of Cardiovascular Diseases, Nanfang Hospital, Southern Medical University, Guangzhou 510515 (China)
Highlights: Black-Right-Pointing-Pointer HSP70 interacts to p38 MAPK in vitro and in vivo. Black-Right-Pointing-Pointer HSP70 co-localizes with p38 MAPK in the nucleus upon stress. Black-Right-Pointing-Pointer HSP70 is involved in the nuclear phosphorylation of MK2 by p38 MAPK. -- Abstract: 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.
- OSTI ID:
- 22210208
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 425, Issue 2; Other Information: Copyright (c) 2012 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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