@Article{Leon_Boulo_Musnier-Activ_GPCR_leads-2014,
  author =	 {Leon, Kelly and Boulo, Thomas and Musnier, Astrid and 
                  Morales, Julia and Gauthier, Christophe and Dupuy, Laurence 
                  and Heyne, Steffen and Backofen, Rolf and Poupon, Anne and 
                  Cormier, Patrick and Reiter, Eric and Crepieux, Pascale},
  title =	 {Activation of a {GPCR} leads to {eIF4G} phosphorylation at 
                  the 5' cap and to {IRES}-dependent translation},
  journal =	 {J Mol Endocrinol},
  year =	 {2014},
  volume =	 {52},
  number =	 {3},
  pages =	 {373-82},
  user =	 {backofen},
  pmid =	 {24711644},
  doi = 	 {10.1530/JME-14-0009},
  issn = 	 {0952-5041},
  issn = 	 {1479-6813},
  abstract =	 {The control of mRNA translation has been mainly explored in 
                  response to activated tyrosine kinase receptors. In 
                  contrast, mechanistic details on the translational machinery 
                  are far less available in the case of ligand-bound G 
                  protein-coupled receptors (GPCRs). In this study, using the 
                  FSH receptor (FSH-R) as a model receptor, we demonstrate 
                  that part of the translational regulations occurs by 
                  phosphorylation of the translation pre-initiation complex 
                  scaffold protein, eukaryotic initiation factor 4G (eIF4G), 
                  in HEK293 cells stably expressing the FSH-R. This 
                  phosphorylation event occurred when eIF4G was bound to the 
                  mRNA 5' cap, and probably involves mammalian target of 
                  rapamycin. This regulation might contribute to cap-dependent 
                  translation in response to FSH. The cap-binding protein 
                  eIF4E also had its phosphorylation level enhanced upon FSH 
                  stimulation. We also show that FSH-induced signaling not 
                  only led to cap-dependent translation but also to internal 
                  ribosome entry site (IRES)-dependent translation of some 
                  mRNA. These data add detailed information on the molecular 
                  bases underlying the regulation of selective mRNA 
                  translation by a GPCR, and a topological model 
                  recapitulating these mechanisms is proposed.}
}