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The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA

Jonathan L E Dean1, Gareth Sully, Andrew R Clark

  • 1Kennedy Institute of Rheumatology Division, Faculty of Medicine, Imperial College London, 1 Aspenlea Rd, Hammersmith, London, W6 8LH, UK. jonathan.dean@imperial.ac.uk

Cellular Signalling
|July 9, 2004
PubMed

Insights

The p38 mitogen-activated protein kinase (MAPK) pathway regulates inflammatory gene expression by controlling mRNA stability. This review examines AU-rich element (ARE)-binding proteins to identify which may mediate p38-dependent mRNA stabilization.

Area of Science:

  • Molecular Biology
  • Immunology
  • Gene Regulation

Background:

  • The p38 MAPK pathway is crucial for post-transcriptional regulation of inflammatory genes.
  • p38 MAPK influences both the translation and stability of inflammatory messenger RNAs (mRNAs).
  • mRNAs targeted by p38 MAPK contain common AU-rich elements (AREs) in their 3'-untranslated regions.

Purpose of the Study:

  • To review AU-rich element (ARE)-binding proteins.
  • To discuss the potential involvement of these proteins in p38-mediated mRNA stabilization.

Main Methods:

  • Literature review of ARE-binding proteins.
  • Analysis of existing research on p38 MAPK signaling and mRNA regulation.

Main Results:

  • AREs are key regulatory sequences in mRNA stability and translation.
  • Multiple proteins, including HuR, TTP, AUF1, and KSRP, bind to AREs.
  • The specific ARE-binding protein responsible for p38-mediated mRNA stabilization remains unidentified.

Conclusions:

  • Understanding the interplay between p38 MAPK and ARE-binding proteins is essential for deciphering inflammatory gene regulation.
  • Further research is needed to pinpoint the exact protein mediating p38-dependent mRNA stabilization.

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