Phosphorylation of the cap-binding protein eIF4E by the MAPK-activated protein kinase Mnk1
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. Consequ...
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| Published in | Biochemical pharmacology Vol. 60; no. 8; pp. 1237 - 1243 |
|---|---|
| Main Author | |
| Format | Journal Article Conference Proceeding |
| Language | English |
| Published |
New York, NY
Elsevier Inc
15.10.2000
Elsevier Science |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0006-2952 1873-2968 |
| DOI | 10.1016/S0006-2952(00)00429-9 |
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| 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. |
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| AbstractList | 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. 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.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. |
| Author | Pyronnet, Stéphane |
| Author_xml | – sequence: 1 givenname: Stéphane surname: Pyronnet fullname: Pyronnet, Stéphane email: Pyronnet@med.mcgill.ca organization: Department of Biochemistry, McGill University, Montreal, Quebec, Canada |
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| Keywords | translation initiation Mnk1 cap binding protein cell cycle phosphorylation Binding protein Signal transduction Phosphorylation Enzyme Protein kinase Transferases Cap structure Initiation factor eIF4E Cell cycle Translation initiation Review |
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| SubjectTerms | Biological and medical sciences cap binding protein cell cycle Cell Cycle - physiology Cell physiology Eukaryotic Initiation Factor-4E Eukaryotic Initiation Factor-4G Fundamental and applied biological sciences. Psychology Humans Intracellular Signaling Peptides and Proteins Mnk1 Molecular and cellular biology Molecular genetics Peptide Initiation Factors - metabolism Peptide Initiation Factors - physiology Phosphorylation Protein Binding Protein-Serine-Threonine Kinases - metabolism RNA Cap-Binding Proteins RNA-Binding Proteins - metabolism Signal transduction translation initiation Translation. Translation factors. Protein processing |
| Title | Phosphorylation of the cap-binding protein eIF4E by the MAPK-activated protein kinase Mnk1 |
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