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Biochem Soc Trans. 2008 Jun;36(Pt 3):491-6. doi: 10.1042/BST0360491.

Control of mRNA decay by phosphorylation of tristetraprolin.

Author information

1
Helmholtz Junior Research Group Post-transcriptional Control of Gene Expression, German Cancer Research Center, DKFZ-ZMBH Alliance, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany.

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.

PMID:
18481987
DOI:
10.1042/BST0360491
[Indexed for MEDLINE]

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