Phosphorylation of TPL-2 on serine 400 is essential for lipopolysaccharide activation of extracellular signal-regulated kinase in macrophages
Molecular and Cellular Biology, ISSN: 0270-7306, Vol: 27, Issue: 21, Page: 7355-7364
2007
- 42Citations
- 52Captures
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Metrics Details
- Citations42
- Citation Indexes42
- 42
- CrossRef41
- Captures52
- Readers52
- 50
Article Description
Tumor progression locus 2 (TPL-2) kinase is essential for Toll-like receptor 4 activation of the mitogen-activated protein kinase extracellular signal-regulated kinase (ERK) and for upregulation of the inflammatory cytokine tumor necrosis factor (TNF) in lipopolysaccharide (LPS)-stimulated macrophages. LPS activation of ERK requires TPL-2 release from associated NF-κB1 p105, which blocks TPL-2 access to its substrate, the ERK kinase MEK. Here we demonstrate that TPL-2 activity is also regulated independently of p105, since LPS stimulation was still needed for TPL-2-dependent activation of ERK in Nfkb1 macrophages. In wild-type macrophages, LPS induced the rapid phosphorylation of serine (S) 400 in the TPL-2 C-terminal tail. Mutation of this conserved residue to alanine (A) blocked the ability of retrovirally expressed TPL-2 to induce the activation of ERK in LPS-stimulated Nfkb1 macrophages. TPL-2 expression also failed to reconstitute LPS activation of ERK and induction of TNF in Map3k8 macrophages, which lack endogenous TPL-2. Consistently, the S400A mutation was found to block LPS stimulation of TPL-2 MEK kinase activity. Thus, induction of TPL-2 MEK kinase activity by LPS stimulation of macrophages requires TPL-2 phosphorylation on S400, in addition to its release from NF-κB1 p105. Oncogenic C-terminal truncations of TPL-2 that remove S400 could promote its transforming potential by eliminating this critical control step. Copyright © 2007, American Society for Microbiology. All Rights Reserved.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=35649024803&origin=inward; http://dx.doi.org/10.1128/mcb.00301-07; http://www.ncbi.nlm.nih.gov/pubmed/17709378; http://mcb.asm.org/cgi/doi/10.1128/MCB.00301-07; https://syndication.highwire.org/content/doi/10.1128/MCB.00301-07; https://www.tandfonline.com/doi/full/10.1128/MCB.00301-07; https://dx.doi.org/10.1128/mcb.00301-07; https://journals.asm.org/doi/10.1128/MCB.00301-07
American Society for Microbiology
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