Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.271.30.17920
Title: Characterization of the structure and function of a new mitogen- activated protein kinase (p38β)
Authors: Jiang, Y.
Chen, C. 
Li, Z.
Guo, W.
Gegner, J.A.
Lin, S. 
Han, J.
Issue Date: 1996
Citation: Jiang, Y., Chen, C., Li, Z., Guo, W., Gegner, J.A., Lin, S., Han, J. (1996). Characterization of the structure and function of a new mitogen- activated protein kinase (p38β). Journal of Biological Chemistry 271 (30) : 17920-17926. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.271.30.17920
Abstract: Mitogen-activated protein (MAP) kinase cascades represent one of the major signal systems used by eukaryotic cells to transduce extracellular signals into cellular responses. Four MAP kinase subgroups have been identified in humans: ERK, JNK (SAPK), ERK5 (BMK), and p38. Here we characterize a new MAP kinase, p38β. p38β is a 372-amino acid protein most closely related to p380. It contains a TGY dual phosphorylation site, which is required for its kinase activity. Like p38, p38β is activated by proinflammatory cytokines and environmental stress. A comparison of events associated with the activation of p38β and p38 revealed differences, most notably in the preferred activation of p38β by MAP kinase kinase 6 (MKK6), whereas p38 was activated nearly equally by MKK3, MKK4, and MKK6. Moreover, in vitro and in vivo experiments showed a strong substrate preference by p38β for activating transcription factor 2 (ATF2). Enhancement of ATF2- dependent gene expression by p38β was ~20-fold greater than that of p38 and other MAP kinases tested. The data reported here suggest that while closely related, p38β and p38 may be regulated by differing mechanisms and may exert their actions on separate downstream targets.
Source Title: Journal of Biological Chemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/116253
ISSN: 00219258
DOI: 10.1074/jbc.271.30.17920
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

623
checked on Jun 17, 2018

WEB OF SCIENCETM
Citations

614
checked on May 16, 2018

Page view(s)

29
checked on May 18, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.