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The Eukaroyotic mRNA Cap Binding Protein (eIF-4E): Phosphorylation and Regulation of Cell Growth

  • R. Frederickson
  • A. Lazaris-Karatzas
  • N. Sonenberg
Conference paper
Part of the NATO ASI Series book series (volume 49)

Abstract

The binding of eukaryotic mRNA to ribosomes requires the participation of at least three initiation factors: eIF-4A, eIF-4B and eIF-4F, and the hydrolysis of ATP (for reviews see Rhoads, 1988; Sonenberg, 1988). A key functional element of the eukaryotic mRNA in this process is the 5′ cap structure, m7GpppN (where N is any nucleotide). This structure facilitates ribosome binding through its interaction with the 24 kDa cap binding protein, termed eIF-4E (Sonenberg et al, 1978). eIF-4E is present in the cell in a free form and in a complex (termed eIF-4F) with two other polypeptides (Tahara et al, 1981; Grifo et al, 1983; Edery et al, 1983). One of these has been identified as eIF-4A, a 50 kDa polypeptide that possesses ATP binding and single-stranded RNA dependent ATPase activities (Sarkar et al, 1985; Abramson et al, 1987), as well as helicase activity in conjunction with eIF-4B (Ray et al, 1985; Rozen et al, 1990). The second of the polypeptides in eIF-4F is a high molecular weight subunit of 220 kDa, termed p220, whose integrity is essential for eIF-4F function (Sonenberg, 1987). eIF-4F stimulates mRNA binding to the 40S ribosomal subunit by unwinding the secondary structure in the mRNA 5′ non-coding region (Ray et al, 1985; Rozen et al, 1990).

Keywords

eUkaryotic Initiation Factor Eukaryotic mRNA Phosphoamino Acid High Molecular Weight Subunit Major Phosphorylation Site 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1990

Authors and Affiliations

  • R. Frederickson
    • 1
  • A. Lazaris-Karatzas
    • 1
  • N. Sonenberg
    • 1
  1. 1.Department of BiochemistryMcGill UniversityMontreal, QuebecCanada

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