Correlation Engine 2.0
Clear Search sequence regions

  • 5 utr (1)
  • cells (1)
  • cellular (2)
  • DAP5 (5)
  • eif 4 (1)
  • eIF2β (2)
  • eif4g (1)
  • eif4g2 protein, human (1)
  • factors (2)
  • humans (1)
  • insights (1)
  • mitosis (1)
  • mrnas (3)
  • nucleic acids (1)
  • protein biosynthesis (1)
  • protein human (1)
  • research (1)
  • ribosome (5)
  • rna caps (2)
  • Sizes of these terms reflect their relevance to your search.

    Initiation is a highly regulated rate-limiting step of mRNA translation. During cap-dependent translation, the cap-binding protein eIF4E recruits the mRNA to the ribosome. Specific elements in the 5'UTR of some mRNAs referred to as Internal Ribosome Entry Sites (IRESes) allow direct association of the mRNA with the ribosome without the requirement for eIF4E. Cap-independent initiation permits translation of a subset of cellular and viral mRNAs under conditions wherein cap-dependent translation is inhibited, such as stress, mitosis and viral infection. DAP5 is an eIF4G homolog that has been proposed to regulate both cap-dependent and cap-independent translation. Herein, we demonstrate that DAP5 associates with eIF2β and eIF4AI to stimulate IRES-dependent translation of cellular mRNAs. In contrast, DAP5 is dispensable for cap-dependent translation. These findings provide the first mechanistic insights into the function of DAP5 as a selective regulator of cap-independent translation. © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.


    Noa Liberman, Valentina Gandin, Yuri V Svitkin, Maya David, Geneviève Virgili, Maritza Jaramillo, Martin Holcik, Bhushan Nagar, Adi Kimchi, Nahum Sonenberg. DAP5 associates with eIF2β and eIF4AI to promote Internal Ribosome Entry Site driven translation. Nucleic acids research. 2015 Apr 20;43(7):3764-75

    Expand section icon Mesh Tags

    Expand section icon Substances

    PMID: 25779044

    View Full Text