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P-body formation is a consequence, not the cause, of RNA-mediated gene silencing

Mol Cell Biol. 2007 Jun;27(11):3970-81. doi: 10.1128/MCB.00128-07. Epub 2007 Apr 2.

Abstract

P bodies are cytoplasmic domains that contain proteins involved in diverse posttranscriptional processes, such as mRNA degradation, nonsense-mediated mRNA decay (NMD), translational repression, and RNA-mediated gene silencing. The localization of these proteins and their targets in P bodies raises the question of whether their spatial concentration in discrete cytoplasmic domains is required for posttranscriptional gene regulation. We show that processes such as mRNA decay, NMD, and RNA-mediated gene silencing are functional in cells lacking detectable microscopic P bodies. Although P bodies are not required for silencing, blocking small interfering RNA or microRNA silencing pathways at any step prevents P-body formation, indicating that P bodies arise as a consequence of silencing. Consistently, we show that releasing mRNAs from polysomes is insufficient to trigger P-body assembly: polysome-free mRNAs must enter silencing and/or decapping pathways to nucleate P bodies. Thus, even though P-body components play crucial roles in mRNA silencing and decay, aggregation into P bodies is not required for function but is instead a consequence of their activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cytoplasmic Structures / genetics
  • Cytoplasmic Structures / metabolism*
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / metabolism
  • Gene Silencing*
  • Humans
  • MicroRNAs / metabolism
  • Polyribosomes / genetics
  • Polyribosomes / metabolism
  • RNA Stability
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism*
  • RNA, Small Interfering / metabolism
  • Ribonucleoproteins / genetics
  • Ribonucleoproteins / metabolism

Substances

  • Drosophila Proteins
  • MicroRNAs
  • RNA, Messenger
  • RNA, Small Interfering
  • Ribonucleoproteins
  • TRAL protein, Drosophila