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Affinity purification of ARE-binding proteins identifies polyA-binding protein 1 as a potential substrate in MK2-induced mRNA stabilization

Item Type:Article
Title:Affinity purification of ARE-binding proteins identifies polyA-binding protein 1 as a potential substrate in MK2-induced mRNA stabilization
Creators Name:Bollig, F. and Winzen, R. and Gaestel, M. and Kostka, S. and Resch, K. and Holtmann, H.
Abstract:An important determinant for the expression level of cytokines and proto-oncogenes is the rate of degradation of their mRNAs. AU-rich sequence elements (AREs) in the 3(') untranslated regions have been found to impose rapid decay of these mRNAs. ARE-containing mRNAs can be stabilized in response to external signals which activate the p38 MAP kinase cascade including the p38 MAP kinase substrate MAPKAP kinase 2 (MK2). In an attempt to identify components downstream of MK2 in this pathway we analyzed several proteins which selectively interact with the ARE of GM-CSF mRNA. One of them, the cytoplasmic poly(A)-binding protein PABP1, co-migrated with a protein that showed prominent phosphorylation by recombinant MK2. Phosphorylation by MK2 was confirmed using PABP1 purified by affinity chromatography on poly(A) RNA. The selective interaction with an ARE-containing RNA and the phosphorylation by MK2 suggest that PABP1 plays a regulatory role in ARE-dependent mRNA decay and its modulation by the p38 MAP kinase cascade.
Keywords:mRNA Stability, AU-Rich Element, Affinity Purification, P38 MAP Kinase, MAPKAP Kinase 2, RNA-Binding Protein, PABP1, Cytokines
Source:Biochemical and Biophysical Research Communications
ISSN:0006-291X
Publisher:Academic Press (U.S.A.)
Volume:301
Number:3
Page Range:665-670
Date:14 February 2003
Official Publication:https://doi.org/10.1016/S0006-291X(03)00015-9
PubMed:View item in PubMed

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