scholarly journals Poly(A)‐Binding Protein Affects the Kinetics of Tobacco Etch Virus Pseudoknot RNA Binding to Wheat germ Translation Initiation Factor eIF4F

2008 ◽  
Vol 22 (S1) ◽  
Author(s):  
Mateen A Khan ◽  
Daniel R Gallie ◽  
Dixie J Goss
Keyword(s):  
Translation Initiation ◽  
Wheat Germ ◽  
Rna Binding ◽  
Binding Protein ◽  
Tobacco Etch Virus ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Kinetics Of

scholarly journals Translation Initiation Factor 4B Homodimerization, RNA Binding, and Interaction with Poly(A)-binding Protein Are Enhanced by Zinc

2008 ◽  
Vol 283 (52) ◽  
pp. 36140-36153 ◽  
Author(s):  
Shijun Cheng ◽  
Shemaila Sultana ◽  
Dixie J. Goss ◽  
Daniel R. Gallie
Keyword(s):  
Translation Initiation ◽  
Rna Binding ◽  
Binding Protein ◽  
Translation Initiation Factor ◽  
Initiation Factor

scholarly journals A specific eIF4A paralog facilitates LARP1-mediated translation repression during mTORC1 inhibition

2021 ◽  
Author(s):  
Yuichi Shichino ◽  
Mari Mito ◽  
Kazuhiro Kashiwagi ◽  
Mari Takahashi ◽  
Takuhiro Ito ◽  
...  
Keyword(s):  
Translation Initiation ◽  
Protein Interactions ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Ribosome Profiling ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Mtor Inhibition ◽  
Translation Repression

AbstractEukaryotic translation initiation factor (eIF) 4A — a DEAD-box RNA-binding protein — plays an essential role in translation initiation. Two mammalian eIF4A paralogs, eIF4A1 and eIF4A2, have been assumed to be redundant because of their high homology, and the difference in their functions has been poorly understood. Here, we show that eIF4A1, but not eIF4A2, enhances translational repression during the inhibition of mechanistic target of rapamycin complex 1 (mTORC1), an essential kinase complex controlling cell proliferation. RNA-immunoprecipitation sequencing (RIP-Seq) of the two eIF4A paralogs revealed that eIF4A1 preferentially binds to mRNAs containing terminal oligopyrimidine (TOP) motifs, whose translation is rapidly repressed upon mTOR inhibition. This biased interaction depends on a La-related RNA-binding protein, LARP1. Ribosome profiling revealed that the deletion of EIF4A1, but not EIF4A2, rendered the translation of TOP mRNAs resistant to mTOR inactivation. Moreover, eIF4A1 enhances the affinity between TOP mRNAs and LARP1 and thus ensures stronger translation repression upon mTORC1 inhibition. Our data show that the distinct protein interactions of these highly homologous translation factor paralogs shape protein synthesis during mTORC1 inhibition and provide a unique example of the repressive role of a universal translation activator.

Effects of pH on kinetics of binding of mRNA-cap analogs by translation initiation factor eIF4E

2003 ◽  
Vol 31 (8) ◽  
pp. 608-616 ◽  
Author(s):  
M. Długosz ◽  
E. Błachut-Okrasińska ◽  
E. Bojarska ◽  
E. Darżynkiewicz ◽  
J. Antosiewicz
Keyword(s):  
Translation Initiation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Effects Of Ph ◽  
Kinetics Of

scholarly journals PLK1 regulates spindle association of phosphorylated eukaryotic translation initiation factor 4E-binding protein and spindle function in mouse oocytes

2017 ◽  
Vol 313 (5) ◽  
pp. C501-C515 ◽  
Author(s):  
Ashley L. Severance ◽  
Keith E. Latham
Keyword(s):  
Translation Initiation ◽  
Binding Protein ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Spindle Formation ◽  
Eukaryotic Translation Initiation Factor ◽  
Eukaryotic Translation ◽  
Chromosome Congression ◽  
Eukaryotic Translation Initiation ◽  
Meiotic Spindles

Oocyte meiotic spindles are associated with spindle-enriched mRNAs, phosphorylated ribosome protein S6, and phosphorylated variants of the key translational regulator, eukaryotic translation initiation factor 4E-binding protein 1 (eIF4E-BP1), consistent with translational control of localized mRNAs by eIF4E-BP1 in facilitating spindle formation and stability. Using specific kinase inhibitors, we determined which kinases regulate phosphorylation status of eIF4E-BP1 associated with meiotic spindles in mouse oocytes and effects of kinase inhibition on chromosome congression and spindle formation. Neither ataxia telangiectasia-mutated kinase nor mechanistic target of rapamycin inhibition significantly affected phosphorylation status of spindle-associated eIF4E-BP1 at the phosphorylation sites examined. Spindle-associated phospho-eIF4E-BP1, spindle formation, and chromosome congression were strongly disrupted by polo-like kinase I (PLK1) inhibition at both metaphase I (MI) and MII. In addition, direct inhibition of eIF4E-BP1 via 4EGI led to spindle defects at MI, indicating a direct role for eIF4E-BP1 phosphorylation in meiotic spindle formation. PLK1 also regulated microtubule dynamics throughout the ooplasm, indicating likely coordination between spindle dynamics and broader ooplasm cytoskeletal dynamics. Because diverse upstream signaling pathways converge on PLK1, these results implicate PLK1 as a major regulatory nexus coupling endogenous and exogenous signals via eIF4E-BP1 to the regulation of spindle formation and stability.

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