Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.274.43.31055
Title: Serine phosphorylation and negative regulation of Stat3 by JNK
Authors: Lim, C.P. 
Cao, X. 
Issue Date: 22-Oct-1999
Citation: Lim, C.P., Cao, X. (1999-10-22). Serine phosphorylation and negative regulation of Stat3 by JNK. Journal of Biological Chemistry 274 (43) : 31055-31061. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.274.43.31055
Abstract: STATs are activated by various cytokines and growth factors via tyrosine phosphorylation, which leads to sequential dimer formation, nuclear translocation, binding to specific DNA sequences, and regulation of gene expression. Recently, serine phosphorylation of Stat3 on Ser-727 by ERK has been identified in response to epidermal growth factor (EGF). Here, we report that Ser727 phosphorylation of Stat3 can also be induced by JNK and activated either by stress or by its upstream kinase and that various stress treatments induce serine phosphorylation of Stat3 in the absence of tyrosine phosphorylation. Inhibitors of ERK and p38 did not inhibit UV-induced Stat3 serine phosphorylation, suggesting that neither of them is involved. We further demonstrate that JNK1, activated by its upstream kinase MKK7, negatively regulated the tyrosine phosphorylation and DNA binding and transcriptional activities of Stat3 stimulated by EGF. Correspondingly, pretreatment of cells with UV reduced the EGF-stimulated tyrosine phosphorylation and phosphotyrosine-dependent activities of Stat3. The inhibitory effect was not observed for Stat1. Our results suggest that Stat3 is a target of JNK that may regulate Stat3 activity via both Ser-727 phosphorylation-dependent and -independent mechanisms.
Source Title: Journal of Biological Chemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/112071
ISSN: 00219258
DOI: 10.1074/jbc.274.43.31055
Appears in Collections:Staff Publications

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

SCOPUSTM   
Citations

179
checked on Dec 5, 2019

WEB OF SCIENCETM
Citations

172
checked on Dec 5, 2019

Page view(s)

45
checked on Nov 29, 2019

Google ScholarTM

Check

Altmetric


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