Abstract
The purpose of this review is to summarize recent experimental data describing the regulation of the phosphorylation of eIF4E, the cap-binding protein, by the MAPK-activated protein kinase Mnk1. Mnk1 does not interact directly with eIF4E, but uses a docking site in eIF4G, a partner of eIF4E. Consequently, control of eIF4E phosphorylation may not strictly depend on changes in Mnk1 activity. The possibility that integrity of the eIF4E/eIF4G/Mnk1 complex also impinges upon eIF4E phosphorylation is discussed.
MeSH terms
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Cell Cycle / physiology
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Eukaryotic Initiation Factor-4E
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Eukaryotic Initiation Factor-4G
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Humans
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Intracellular Signaling Peptides and Proteins
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Peptide Initiation Factors / metabolism*
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Peptide Initiation Factors / physiology
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Phosphorylation
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Protein Binding
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Protein Serine-Threonine Kinases / metabolism*
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RNA Cap-Binding Proteins
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RNA-Binding Proteins / metabolism*
Substances
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Eukaryotic Initiation Factor-4E
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Eukaryotic Initiation Factor-4G
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Intracellular Signaling Peptides and Proteins
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Peptide Initiation Factors
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RNA Cap-Binding Proteins
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RNA-Binding Proteins
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MKNK1 protein, human
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Protein Serine-Threonine Kinases