mTORC1 and CK2 coordinate ternary and eIF4F complex assembly - Biological Adaptation and Ageing Accéder directement au contenu
Article Dans Une Revue Nature Communications Année : 2016

mTORC1 and CK2 coordinate ternary and eIF4F complex assembly

Olivier Jean-Jean

Résumé

Ternary complex (TC) and eIF4F complex assembly are the two major rate-limiting steps in translation initiation regulated by eIF2α phosphorylation and the mTOR/4E-BP pathway, respectively. How TC and eIF4F assembly are coordinated, however, remains largely unknown. We show that mTOR suppresses translation of mRNAs activated under short-term stress wherein TC recycling is attenuated by eIF2α phosphorylation. During acute nutrient or growth factor stimulation, mTORC1 induces eIF2β phosphorylation and recruitment of NCK1 to eIF2, decreases eIF2α phosphorylation and bolsters TC recycling. Accordingly, eIF2β mediates the effect of mTORC1 on protein synthesis and proliferation. In addition, we demonstrate a formerly undocumented role for CK2 in regulation of translation initiation, whereby CK2 stimulates phosphorylation of eIF2β and simultaneously bolsters eIF4F complex assembly via the mTORC1/4E-BP pathway. These findings imply a previously unrecognized mode of translation regulation, whereby mTORC1 and CK2 coordinate TC and eIF4F complex assembly to stimulate cell proliferation.
Fichier principal
Vignette du fichier
ncomms11127.pdf (2.79 Mo) Télécharger le fichier
Origine : Publication financée par une institution
Loading...

Dates et versions

hal-01299782 , version 1 (08-04-2016)

Licence

Paternité

Identifiants

Citer

Valentina Gandin, Laia Masvidal, Marie Cargnello, Laszlo Gyenis, Shannon Mclaughlan, et al.. mTORC1 and CK2 coordinate ternary and eIF4F complex assembly. Nature Communications, 2016, 7, pp.11127. ⟨10.1038/ncomms11127⟩. ⟨hal-01299782⟩
593 Consultations
197 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More