New insights on the interaction between the isoforms 1 and 2 of human translation elongation factor 1A
| Autor: | Annalisa Lamberti, Nicola M. Martucci, Paolo Arcari, Salvatore Arbucci, Carmen Sanges, Nunzia Migliaccio, Emilia Rippa, Rosarita Tatè, Immacolata Ruggiero |
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| Přispěvatelé: | Migliaccio, Nunzia, Ruggiero, Immacolata, Martucci, NICOLA MASSIMILIANO, Sanges, Carmen, Arbucci, Salvatore, Tatè, Rosarita, Rippa, Emilia, Arcari, Paolo, Lamberti, Annalisa |
| Rok vydání: | 2015 |
| Předmět: |
Protein moonlighting
Blotting Western EEF1A2 Biology Transfection Biochemistry Peptide Elongation Factor 1 Eukaryotic translation Chlorocebus aethiops Fluorescence Resonance Energy Transfer Protein biosynthesis Animals Humans Eukaryotic translation elongation factor 1A (eEF1A) Cellular localization Microscopy Confocal Crosslinking Chimera General Medicine Eukaryotic translation elongation factor 1 alpha 1 Cell biology Confocal microscopy Elongation factor COS Cells FRET Phosphorylation |
| Zdroj: | Biochimie 118 (2015): 1–7. doi:10.1016/j.biochi.2015.07.021 info:cnr-pdr/source/autori:Migliaccio, Nunzia; Ruggiero, Immacolata; Martucci, Nicola M.; Sanges, Carmen; Arbucci, Salvatore; Tate, Rosarita; Rippa, Emilia; Arcari, Paolo; Lamberti, Annalisa/titolo:New insights on the interaction between the isoforms 1 and 2 of human translation elongation factor 1A/doi:10.1016%2Fj.biochi.2015.07.021/rivista:Biochimie (Print)/anno:2015/pagina_da:1/pagina_a:7/intervallo_pagine:1–7/volume:118 |
| ISSN: | 0300-9084 |
| DOI: | 10.1016/j.biochi.2015.07.021 |
| Popis: | The eukaryotic translation elongation factor 1A (eEF1A) is a moonlighting protein that besides to its canonical role in protein synthesis is also involved in many other cellular processes such as cell survival and apoptosis. In a previous work, we identified eEF1A Raf-mediated phosphorylation sites and defined their role in the regulation of eEF1A half-life and apoptosis of human cancer cells. We proposed that the phosphorylation of eEF1A by C-Raf required the presence of both eEF1A isoforms thus suggesting the formation of a potential eEF1A heterodimer owning regulatory properties. This study aimed at investigating the cellular localization and interaction between two eEF1A isoforms. To this end, we developed chimera proteins by adding at the N-terminal end of both eEF1A1 and eEF1A2 cyan fluorescence protein (mCerulean) and yellow fluorescence protein (mVenus), respectively. The fluorescent eEF1A1 and eEF1A2 chimeras were both addressed to COS-7 cells and found co-localized in the cytoplasm at the level of cellular membranes. We highlighted FRET between the labeled N-termini of eEF1A isoforms. The intramolecular FRET of this chimera was about 17%. Our results provide novel information on the intracellular distribution and interaction of eEF1A isoforms. (C) 2015 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved. |
| Databáze: | OpenAIRE |
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