scholarly journals The eukaryotic initiation factor 4E (eIF4E) binding domain of eIF4GI enhances recruitment and discrimination among a subset of mRNAs containing structured 5’UTRs

2021 ◽  
Vol 35 (S1) ◽  
Author(s):  
Baishakhi Saha ◽  
Solomon Haizel ◽  
Usha Bhardwaj ◽  
Dixie Goss
Keyword(s):  
Binding Domain ◽  
Initiation Factor ◽  
Eukaryotic Initiation Factor ◽  
Eukaryotic Initiation Factor 4E

scholarly journals Phosphorylation of eukaryotic initiation factor 4E (eIF4E) at Ser209 is not required for protein synthesis in vitro and in vivo

2001 ◽  
Vol 268 (20) ◽  
pp. 5375-5385 ◽  
Author(s):  
Linda McKendrick ◽  
Simon J. Morley ◽  
Virginia M. Pain ◽  
Rosemary Jagus ◽  
Bhavesh Joshi
Keyword(s):  
Protein Synthesis ◽  
Initiation Factor ◽  
Eukaryotic Initiation Factor ◽  
Eukaryotic Initiation Factor 4E

scholarly journals Identification of a Nucleic Acid Binding Domain in Eukaryotic Initiation Factor eIFiso4G from Wheat

1999 ◽  
Vol 274 (15) ◽  
pp. 10603-10608 ◽  
Author(s):  
Chang-Yub Kim ◽  
Katsuyuki Takahashi ◽  
Tran B. Nguyen ◽  
Justin K. M. Roberts ◽  
Cecelia Webster
Keyword(s):  
Nucleic Acid ◽  
Binding Domain ◽  
Initiation Factor ◽  
Eukaryotic Initiation Factor ◽  
Nucleic Acid Binding

Thermodynamics of Molecular Recognition of mRNA 5′ Cap by Yeast Eukaryotic Initiation Factor 4E

2011 ◽  
Vol 115 (27) ◽  
pp. 8746-8754 ◽  
Author(s):  
Katarzyna Kiraga-Motoszko ◽  
Anna Niedzwiecka ◽  
Anna Modrak-Wojcik ◽  
Janusz Stepinski ◽  
Edward Darzynkiewicz ◽  
...  
Keyword(s):  
Molecular Recognition ◽  
Initiation Factor ◽  
Eukaryotic Initiation Factor ◽  
Eukaryotic Initiation Factor 4E

Tissue Distribution, Genomic Structure, and Chromosome Mapping of Mouse and Human Eukaryotic Initiation Factor 4E-Binding Proteins 1 and 2

Genomics ◽  
1996 ◽  
Vol 38 (3) ◽  
pp. 353-363 ◽  
Author(s):  
Kyoko Tsukiyama-Kohara ◽  
Silvia M. Vidal ◽  
Anne-Claude Gingras ◽  
Thomas W. Glover ◽  
Samir M. Hanash ◽  
...  
Keyword(s):  
Tissue Distribution ◽  
Binding Proteins ◽  
Genomic Structure ◽  
Chromosome Mapping ◽  
Initiation Factor ◽  
Eukaryotic Initiation Factor ◽  
Eukaryotic Initiation Factor 4E

scholarly journals Eukaryotic Initiation Factor 4E Binding Protein Family of Proteins: Sentinels at a Translational Control Checkpoint in Lung Tumor Defense

2009 ◽  
Vol 69 (21) ◽  
pp. 8455-8462 ◽  
Author(s):  
Yong Y. Kim ◽  
Linda Von Weymarn ◽  
Ola Larsson ◽  
Danhua Fan ◽  
Jon M. Underwood ◽  
...  
Keyword(s):  
Translational Control ◽  
Lung Tumor ◽  
Binding Protein ◽  
Protein Family ◽  
Initiation Factor ◽  
Eukaryotic Initiation Factor ◽  
Eukaryotic Initiation Factor 4E

scholarly journals Cap-binding protein (eukaryotic initiation factor 4E) and 4E-inactivating protein BP-1 independently regulate cap-dependent translation.

1996 ◽  
Vol 16 (10) ◽  
pp. 5450-5457 ◽  
Author(s):  
D Feigenblum ◽  
R J Schneider
Keyword(s):  
Heat Shock ◽  
Translation Initiation ◽  
Binding Protein ◽  
Initiation Factor ◽  
Eukaryotic Initiation Factor ◽  
Metaphase Arrest ◽  
Animal Cells ◽  
Eukaryotic Initiation Factor 4E ◽  
Dependent Protein

Cap-dependent protein synthesis in animal cells is inhibited by heat shock, serum deprivation, metaphase arrest, and infection with certain viruses such as adenovirus (Ad). At a mechanistic level, translation of capped mRNAs is inhibited by dephosphorylation of eukaryotic initiation factor 4E (eIF-4E) (cap-binding protein) and its physical sequestration with the translation repressor protein BP-1 (PHAS-I). Dephosphorylation of BP-I blocks cap-dependent translation by promoting sequestration of eIF-4E. Here we show that heat shock inhibits translation of capped mRNAs by simultaneously inducing dephosphorylation of eIF-4E and BP-1, suggesting that cells might coordinately regulate translation of capped mRNAs by impairing both the activity and the availability of eIF-4E. Like heat shock, late Ad infection is shown to induce dephosphorylation of eIF-4E. However, in contrast to heat shock, Ad also induces phosphorylation of BP-1 and release of eIF-4E. BP-1 and eIF-4E can therefore act on cap-dependent translation in either a mutually antagonistic or cooperative manner. Three sets of experiments further underscore this point: (i) rapamycin is shown to block phosphorylation of BP-1 without inhibiting dephosphorylation of eIF-4E induced by heat shock or Ad infection, (ii) eIF-4E is efficiently dephosphorylated during heat shock or Ad infection regardless of whether it is in a complex with BP-1, and (iii) BP-1 is associated with eIF-4E in vivo regardless of the state of eIF-4E phosphorylation. These and other studies establish that inhibition of cap-dependent translation does not obligatorily involve sequestration of eIF-4E by BP-1. Rather, translation is independently regulated by the phosphorylation states of eIF-4E and the 4E-binding protein, BP-1. In addition, these results demonstrate that BP-1 and eIF-4E can act either in concert or in opposition to independently regulate cap-dependent translation. We suggest that independent regulation of eIF-4E and BP-1 might finely regulate the efficiency of translation initiation or possibly control cap-dependent translation for fundamentally different purposes.

Crystallization and Preliminary X-Ray Diffraction Study of Recombinant Human Eukaryotic Initiation Factor-4E

1996 ◽  
Vol 119 (2) ◽  
pp. 224-225 ◽  
Author(s):  
S. Morino ◽  
K. Tomoo ◽  
N. Nishi ◽  
K. Okabe ◽  
M. Doi ◽  
...  
Keyword(s):  
Diffraction Study ◽  
Initiation Factor ◽  
Eukaryotic Initiation Factor ◽  
X Ray Diffraction ◽  
X Ray ◽  
Eukaryotic Initiation Factor 4E
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