Gene suppression by tristetraprolin and release by the p38 pathway.

@article{Zhu2001GeneSB,
  title={Gene suppression by tristetraprolin and release by the p38 pathway.},
  author={W. Zhu and Michael Brauchle and Franco E. Di Padova and Hermann Gram and Liguo New and Koh Ono and Jocelyn S. Downey and J. Han},
  journal={American journal of physiology. Lung cellular and molecular physiology},
  year={2001},
  volume={281 2},
  pages={
          L499-508
        }
}
  • W. Zhu, M. Brauchle, +5 authors J. Han
  • Published 1 August 2001
  • Biology
  • American journal of physiology. Lung cellular and molecular physiology
Tristetraprolin (TTP) is a zinc finger protein that has been implicated in the control of tumor necrosis factor (TNF) mRNA stability. We show here that TTP protein has a suppressive effect on promoter elements from TNF-alpha and interleukin-8 and that lipopolysaccharide (LPS) stimulation can release this suppression. The release in LPS-stimulated cells was found to be primarily mediated by the p38 pathway because activation of p38 is sufficient to remove the suppressive effect of TTP. Indeed… 
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The Stability of Tristetraprolin mRNA Is Regulated by Mitogen-activated Protein Kinase p38 and by Tristetraprolin Itself*
TLDR
It is shown that TTP mRNA is expressed in a biphasic manner following stimulation of cells with lipopolysaccharide and that the second phase of expression, like the first, is dependent on mitogen-activated protein kinase (MAPK) p38.
Dominant Suppression of Inflammation via Targeted Mutation of the mRNA Destabilizing Protein Tristetraprolin
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The equilibrium between unphosphorylated and phosphorylated TTP is a critical determinant of the inflammatory response, and manipulation of this equilibrium may be a means of treating inflammatory pathologies.
Inhibition of tristetraprolin expression by dexamethasone in activated macrophages.
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TLDR
The cytoplasmic location of TTP is established, supporting a major role for this protein in regulating TNF production, and suggesting that TTP levels are not regulated solely by TNF.
Regulation of tristetraprolin expression by mitogen‐activated protein kinase phosphatase‐1
TLDR
This study investigated the role of MKP‐1 in TTP expression in A549 human lung epithelial cells, THp‐1 human macrophages, J774 mouse macrophage, and primary mouse Macrophages and suppressed TTPexpression by inhibiting p38 MAPK pathway.
Phosphorylation of Recombinant Tristetraprolin In vitro
TLDR
Results demonstrate that TTP is a substrate for a number of protein kinases in vitro, including GSK3b, PKA, PKB, PKC, and JNK.
Multiple tristetraprolin sequence domains required to induce apoptosis and modulate responses to TNFα through distinct pathways
TLDR
It is shown that other regions of TTP along with the zinc fingers are required for TTP to induce apoptosis, and that modulation of TNFα responses may be a unique and important aspect of T TP function.
The role of tristetraprolin in cancer and inflammation.
TLDR
This review summarizes the current understanding of post-transcriptional regulation of ARE-containing gene expression by TTP and discusses its role in maintaining homeostasis and the pathological consequences of losing TTP expression.
The Role of mRNA Turnover in the Regulation of Tristetraprolin Expression: Evidence for an Extracellular Signal-Regulated Kinase-Specific, AU-Rich Element-Dependent, Autoregulatory Pathway1
TLDR
TTP regulates its own expression in a manner identical to that seen with the TNF-α 3′ untranslated region, indicating that this autoregulation is mediated at the level of mRNA stability.
PARP-14 combines with tristetraprolin in the selective posttranscriptional control of macrophage tissue factor expression.
TLDR
A novel mechanism for the posttranscriptional regulation of TF expression is provided, indicating that this is selectively regulated by PARP-14.
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References

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