TTP (tristetraprolin) is an RNA-binding protein that suppresses inflammation by accelerating the degradation of cytokine mRNAs. TTP binds to an AU-rich element in the 3′-untranslated region of its target mRNAs. In macrophages, the induction of cytokine expression requires activation of the p38-MAPK (mitogen-activated protein kinase)–MK2 [MAPKAP (MAPK-activated protein) kinase-2] kinase cascade. MK2 directly phosphorylates TTP and thereby contributes to transient stabilization of cytokine mRNAs. In the present review, we address the target specificity of TTP, summarize TTP-interacting proteins and discuss how phosphorylation regulates the activity, localization and stability of TTP.
Conference Article| May 21 2008
Control of mRNA decay by phosphorylation of tristetraprolin
Georg Stoecklin 1
1Helmholtz Junior Research Group Post-transcriptional Control of Gene Expression, German Cancer Research Center, DKFZ-ZMBH Alliance, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany
1To whom correspondence should be addressed (email email@example.com).
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Heike Sandler, Georg Stoecklin; Control of mRNA decay by phosphorylation of tristetraprolin. Biochem Soc Trans 1 June 2008; 36 (3): 491–496. doi: https://doi.org/10.1042/BST0360491
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