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Control of mRNA decay by heat shock-ubiquitin-proteasome pathway.

Cytokine and proto-oncogene messenger RNAs (mRNAs) are rapidly degraded through AU-rich elements in the 3' untranslated region. Rapid decay involves AU-rich binding protein AUF1, which complexes with heat shock proteins hsc70-hsp70, translation initiation factor eIF4G, and poly(A) binding protein. AU-rich mRNA decay is associated with displacement of eIF4G from AUF1, ubiquitination of AUF1, and degradation of AUF1 by proteasomes. Induction of hsp70 by heat shock, down-regulation of the ubiquitin-proteasome network, or inactivation of ubiquitinating enzyme E1 all result in hsp70 sequestration of AUF1 in the perinucleus-nucleus, and all three processes block decay of AU-rich mRNAs and AUF1 protein. These results link the rapid degradation of cytokine mRNAs to the ubiquitin-proteasome pathway.

Pubmed ID: 10205060

Authors

  • Laroia G
  • Cuesta R
  • Brewer G
  • Schneider RJ

Journal

Science (New York, N.Y.)

Publication Data

April 16, 1999

Associated Grants

  • Agency: NCI NIH HHS, Id: CA42357
  • Agency: NCI NIH HHS, Id: CA52443

Mesh Terms

  • 3' Untranslated Regions
  • Carrier Proteins
  • Cell Nucleus
  • Cysteine Endopeptidases
  • Cysteine Proteinase Inhibitors
  • Cytoplasm
  • Eukaryotic Initiation Factor-4G
  • Granulocyte-Macrophage Colony-Stimulating Factor
  • HSC70 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins
  • HeLa Cells
  • Heat-Shock Response
  • Heterogeneous-Nuclear Ribonucleoprotein D
  • Humans
  • Leupeptins
  • Multienzyme Complexes
  • Peptide Initiation Factors
  • Poly(A)-Binding Proteins
  • Proteasome Endopeptidase Complex
  • Protein Binding
  • RNA, Messenger
  • RNA-Binding Proteins
  • Transfection
  • Ubiquitins