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

Science (New York, N.Y.) | Apr 16, 1999

http://www.ncbi.nlm.nih.gov/pubmed/10205060

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 RIS Download

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

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Associated grants

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

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