scholarly journals Synthetic Polyamines to Regulate mRNA Translation through the Preservative Binding of Eukaryotic Initiation Factor 4E to the Cap Structure

2016 ◽  
Vol 138 (5) ◽  
pp. 1478-1481 ◽  
Author(s):  
Hirokuni Uchida ◽  
Keiji Itaka ◽  
Satoshi Uchida ◽  
Takehiko Ishii ◽  
Tomoya Suma ◽  
...  
Keyword(s):  
Mrna Translation ◽  
Initiation Factor ◽  
Eukaryotic Initiation Factor ◽  
Eukaryotic Initiation Factor 4E ◽  
Synthetic Polyamines

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

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

scholarly journals Multiple Mechanisms Control Phosphorylation of PHAS-I in Five (S/T)P Sites That Govern Translational Repression

2000 ◽  
Vol 20 (10) ◽  
pp. 3558-3567 ◽  
Author(s):  
Isabelle Mothe-Satney ◽  
Daqing Yang ◽  
Patrick Fadden ◽  
Timothy A. J. Haystead ◽  
John C. Lawrence
Keyword(s):  
Mrna Translation ◽  
Hek293 Cells ◽  
Initiation Factor ◽  
Translational Repression ◽  
Phosphorylation Sites ◽  
Translational Repressor ◽  
Eukaryotic Initiation Factor 4E ◽  
Dependent Processes ◽  
Constitutive Phosphorylation

ABSTRACT Control of the translational repressor, PHAS-I, was investigated by expressing proteins with Ser/Thr → Ala mutations in the five (S/T)P phosphorylation sites. Results of experiments with HEK293 cells reveal at least three levels of control. At one extreme is nonregulated phosphorylation, exemplified by constitutive phosphorylation of Ser82. At an intermediate level, amino acids and insulin stimulate the phosphorylation of Thr36, Thr45, and Thr69 via mTOR-dependent processes that function independently of other sites in PHAS-I. At the third level, the extent of phosphorylation of one site modulates the phosphorylation of another. This control is represented by Ser64 phosphorylation, which depends on the phosphorylation of all three TP sites. The five sites have different influences on the electrophoretic properties of PHAS-I and on the affinity of PHAS-I for eukaryotic initiation factor 4E (eIF4E). Phosphorylation of Thr45 or Ser64 results in the most dramatic decreases in eIF4E binding in vitro. However, each of the sites influences mRNA translation, either directly by modulating the binding affinity of PHAS-I and eIF4E or indirectly by affecting the phosphorylation of other sites.

4E-BP1 and S6K1: translational integration sites for nutritional and hormonal information in muscle

2000 ◽  
Vol 279 (4) ◽  
pp. E715-E729 ◽  
Author(s):  
O. Jameel Shah ◽  
Joshua C. Anthony ◽  
Scot R. Kimball ◽  
Leonard S. Jefferson
Keyword(s):  
Translational Control ◽  
Mrna Translation ◽  
Cellular Protein ◽  
Initiation Factor ◽  
Translational Repressor ◽  
Initiation Factors ◽  
Initiation Phase ◽  
Eukaryotic Initiation Factor 4E ◽  
Integration Sites ◽  
A Site

Maintenance of cellular protein stores in skeletal muscle depends on a tightly regulated synthesis-degradation equilibrium that is conditionally modulated under an extensive range of physiological and pathophysiological circumstances. Recent studies have established the initiation phase of mRNA translation as a pivotal site of regulation for global rates of protein synthesis, as well as a site through which the synthesis of specific proteins is controlled. The protein synthetic pathway is exquisitely sensitive to the availability of hormones and nutrients and employs a comprehensive integrative strategy to interpret the information provided by hormonal and nutritional cues. The translational repressor, eukaryotic initiation factor 4E binding protein 1 (4E-BP1), and the 70-kDa ribosomal protein S6 kinase (S6K1) have emerged as important components of this strategy, and together they coordinate the behavior of both eukaryotic initiation factors and the ribosome. This review discusses the role of 4E-BP1 and S6K1 in translational control and outlines the mechanisms through which hormones and nutrients effect changes in mRNA translation through the influence of these translational effectors.

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
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