Turnover of AU-rich-containing mRNAs during stress: a matter of survival

Wiley Interdiscip Rev RNA. 2011 May-Jun;2(3):336-47. doi: 10.1002/wrna.55. Epub 2010 Oct 19.

Abstract

Cells undergo various adaptive measures in response to stress. Among these are specific changes in the posttranscriptional regulation of various genes. In particular, the turnover of mRNA is modified to either increase or decrease the abundance of certain target messages. Some of the best-studied mRNAs that are affected by stress are those that contain adenine/uridine-rich elements (AREs) in their 3'-untranslated regions. ARE-containing mRNAs are involved in many important cellular processes and are normally labile, but in response to stress they are differentially regulated through the concerted efforts of ARE-binding proteins (AUBPs) such as HuR, AUF1, tristetraprolin, BRF1, and KSRP, along with microRNA-mediated effects. Additionally, the fate of ARE-containing mRNAs is modified by inducing their localization to stress granules or mRNA processing bodies. Coordination of these various mechanisms controls the turnover of ARE-containing mRNAs, and thereby enables proper responses to cellular stress. In this review, we discuss how AUBPs regulate their target mRNAs in response to stress, along with the involvement of cytoplasmic granules in this process.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • 3' Untranslated Regions
  • Adenine / chemistry
  • Base Composition
  • Cytoplasmic Granules / metabolism
  • ELAV Proteins / metabolism
  • MicroRNAs / metabolism
  • Models, Biological
  • RNA Processing, Post-Transcriptional
  • RNA Stability
  • RNA, Messenger / chemistry
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism*
  • RNA-Binding Proteins / metabolism
  • Stress, Physiological
  • Tristetraprolin / metabolism
  • Uracil / chemistry

Substances

  • 3' Untranslated Regions
  • ELAV Proteins
  • MicroRNAs
  • RNA, Messenger
  • RNA-Binding Proteins
  • Tristetraprolin
  • adenine-uracil dimers
  • Uracil
  • Adenine