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A reinvestigation of the multisite phosphorylation of the transcription factor c‐Jun

A reinvestigation of the multisite phosphorylation of the transcription factor c‐Jun We have used phospho‐specific antibodies to re‐examine the multisite phosphorylation of c‐Jun in murine RAW macrophages and embryonic fibroblasts. Our results indicate that JNK isoforms are required and sufficient for the phosphorylation of Thr91 and Thr93, as well as the phosphorylation of Ser63 and Ser73, in response to LPS or anisomycin in macrophages and TNFα or anisomycin in fibroblasts. However, the phorbol ester (TPA) and EGF‐induced phosphorylation of Ser63 and Ser73 is mediated by ERK1/ERK2, as well as JNK1/JNK2, in fibroblasts from wild‐type mice and by ERK1/ERK2 alone in fibroblasts from JNK‐deficient mice. The phosphorylation of Thr239 is catalysed by GSK3 and the phosphorylation of Ser243 by an as yet unidentified protein kinase. The inhibition of GSK3 is not required for the dephosphorylation of Thr239 in response to LPS, and nor is the phosphorylation of Thr91 and Thr93 required for the TPA‐ or EGF‐induced dephosphorylation of Thr239 in fibroblasts. The agonist‐induced dephosphorylation of Thr239 may involve a conformational change that exposes Thr239 to dephosphorylation and/or the activation of a Thr239 phosphatase. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The EMBO Journal Wiley

A reinvestigation of the multisite phosphorylation of the transcription factor c‐Jun

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References (31)

Publisher
Wiley
Copyright
Copyright © 2013 Wiley Periodicals, Inc
ISSN
0261-4189
eISSN
1460-2075
DOI
10.1093/emboj/cdg388
pmid
12881422
Publisher site
See Article on Publisher Site

Abstract

We have used phospho‐specific antibodies to re‐examine the multisite phosphorylation of c‐Jun in murine RAW macrophages and embryonic fibroblasts. Our results indicate that JNK isoforms are required and sufficient for the phosphorylation of Thr91 and Thr93, as well as the phosphorylation of Ser63 and Ser73, in response to LPS or anisomycin in macrophages and TNFα or anisomycin in fibroblasts. However, the phorbol ester (TPA) and EGF‐induced phosphorylation of Ser63 and Ser73 is mediated by ERK1/ERK2, as well as JNK1/JNK2, in fibroblasts from wild‐type mice and by ERK1/ERK2 alone in fibroblasts from JNK‐deficient mice. The phosphorylation of Thr239 is catalysed by GSK3 and the phosphorylation of Ser243 by an as yet unidentified protein kinase. The inhibition of GSK3 is not required for the dephosphorylation of Thr239 in response to LPS, and nor is the phosphorylation of Thr91 and Thr93 required for the TPA‐ or EGF‐induced dephosphorylation of Thr239 in fibroblasts. The agonist‐induced dephosphorylation of Thr239 may involve a conformational change that exposes Thr239 to dephosphorylation and/or the activation of a Thr239 phosphatase.

Journal

The EMBO JournalWiley

Published: Jan 1, 2003

Keywords: ; ; ; ;

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