Phosphorylation of Eukaryotic Translation Initiation Factor 4G1 (eIF4G1) by Protein Kinase Cα Regulates eIF4G1 Binding to Mnk1▿
| Autor: | Mikhail I. Dobrikov, Matthias Gromeier, Elena Y. Dobrikova, Mayya Shveygert |
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| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
Protein Kinase C-alpha
Recombinant Fusion Proteins Molecular Sequence Data Biology Protein Serine-Threonine Kinases chemistry.chemical_compound Eukaryotic initiation factor Phorbol Esters Initiation factor Animals Humans Amino Acid Sequence Enzyme Inhibitors Phosphorylation Extracellular Signal-Regulated MAP Kinases Molecular Biology eIF2 EIF4G EIF4E Intracellular Signaling Peptides and Proteins Cell Biology EIF4A1 Articles Eukaryotic translation initiation factor 4 gamma Cell biology Enzyme Activation Isoenzymes EIF4EBP1 HEK293 Cells chemistry Biochemistry ras Proteins Eukaryotic Initiation Factor-4G Protein Binding Signal Transduction |
| Popis: | Signal transduction through mitogen-activated protein kinases (MAPKs) is implicated in growth and proliferation control through translation regulation and involves posttranslational modification of translation initiation factors. For example, convergent MAPK signals to Mnk1 lead to phosphorylation of eukaryotic translation initiation factor 4E (eIF4E), which has been linked to malignant transformation. However, understanding the compound effects of mitogenic signaling on the translation apparatus and on protein synthesis control remains elusive. This is particularly true for the central scaffold of the translation initiation apparatus and ribosome adaptor eIF4G. To unravel the effects of signal transduction to eIF4G on translation, we used specific activation of protein kinase C (PKC)-Ras-Erk signaling with phorbol esters. Phospho-proteomic and mutational analyses revealed that eIF4G1 is a substrate for PKCα at Ser1186. We show that PKCα activation elicits a cascade of orchestrated phosphorylation events that may modulate eIF4G1 structure and control interaction with the eIF4E kinase, Mnk1. |
| Databáze: | OpenAIRE |
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