Control of mRNA decay by phosphorylation of tristetraprolin - PubMed (original) (raw)

Review

. 2008 Jun;36(Pt 3):491-6.

doi: 10.1042/BST0360491.

Affiliations

• PMID: 18481987
• DOI: 10.1042/BST0360491

Review

Control of mRNA decay by phosphorylation of tristetraprolin

Heike Sandler et al. Biochem Soc Trans. 2008 Jun.

Abstract

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.

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