These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Characterization of wild-type and Ser53 mutant eukaryotic initiation factor 4E overexpression in mammalian cells.
    Author: Kaufman RJ, Murtha-Riel P, Pittman DD, Davies MV.
    Journal: J Biol Chem; 1993 Jun 05; 268(16):11902-9. PubMed ID: 8505316.
    Abstract:
    Eukaryotic translation initiation factor 4E (eIF-4E) is one component of the m7G-cap-binding protein complex eIF-4F and is required for cap-dependent translation initiation. The phosphorylation state of eIF-4E correlates with increased activity and a major phosphorylation site resides at serine 53. To further evaluate the role of eIF-4E phosphorylation, eIF-4E wild-type and two Ser53 mutants, Ser53Ala and Ser53Asp, were expressed at high level, representing almost 2% of the total cell protein, by transient transfection of COS-1 monkey cells. 32PO4 metabolic labeling of transfected cells demonstrated both Ser53 mutants were phosphorylated at an alternate serine residue. [35S]Methionine pulse-labeling demonstrated that the wild-type and both Ser53 mutants were equally incorporated into the eIF-4F complex. The effect of wild-type and Ser53 mutant overexpression on cap-dependent translation initiation and internal translation initiation was monitored by cotransfection with an expression vector encoding a dicistronic mRNA for which the 5' cistron is translated in a cap-dependent manner, and the 3' cistron is translated by internal ribosome binding. Unexpectedly, overexpression of the wild-type or either mutant did not affect the efficiency of either cap-dependent or internal initiation. These results demonstrate that phosphorylation of eIF-4E at residue 53 is not required for interaction with p220 and suggest that Ser53 phosphorylation may not be required for cap-dependent translation initiation in this system.
    [Abstract] [Full Text] [Related] [New Search]