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CUG-BP binds to RNA substrates and recruits PARN deadenylase

Karen C M Moraes1, Carol J Wilusz, Jeffrey Wilusz

  • 1Department of Microbiology, Immunology & Pathology, College of Veterinary Medicine & Biomedical Sciences, Colorado State University, Fort Collins, 80523, USA.

RNA (New York, N.Y.)
|April 8, 2006
PubMed

Insights

Cytoplasmic polyadenylation element-binding protein (CUG-BP) directly recruits the deadenylase PARN to target mRNAs, initiating mRNA decay. This study reveals CUG-BP

Area of Science:

  • Molecular Biology
  • RNA Metabolism
  • Gene Regulation

Background:

  • CUG-BP, a homolog of Xenopus EDEN-BP, binds to mRNAs like c-mos, influencing deadenylation post-fertilization.
  • Previous research highlighted CUG-BP's roles in splicing and translation regulation in mammals.
  • CUG-BP's specific involvement in mRNA decay pathways remained largely unexamined.

Purpose of the Study:

  • To investigate the role of CUG-BP in the mRNA decay process.
  • To dissect the function of CUG-BP in the deadenylation of specific ARE-containing mRNAs (c-fos and TNFalpha).

Main Methods:

  • In vitro deadenylation assays were employed to study mRNA decay.
  • RNA-binding specificity of CUG-BP was assessed.
  • Coimmunoprecipitation assays were used to examine protein-protein interactions between CUG-BP and PARN.

Main Results:

  • CUG-BP specifically binds to both c-fos and TNFalpha mRNAs.
  • CUG-BP enhances poly(A) tail shortening mediated by PARN.
  • Coimmunoprecipitation confirmed an interaction between CUG-BP and PARN, reproducible with recombinant proteins.

Conclusions:

  • CUG-BP is identified as the first RNA-binding protein capable of directly recruiting a deadenylase (PARN) to an RNA substrate.
  • This interaction facilitates the initiation of mRNA decay.
  • CUG-BP plays a direct role in regulating mRNA stability through deadenylation.

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