Phosphorylation of b-arrestin2 at Thr 383 by MEK underlies b-arrestin-dependent activation of Erk1/2 by GPCRs - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue eLife Année : 2017

Phosphorylation of b-arrestin2 at Thr 383 by MEK underlies b-arrestin-dependent activation of Erk1/2 by GPCRs

Résumé

In addition to their role in desensitization and internalization of G protein-coupled receptors (GPCRs), b-arrestins are essential scaffolds linking GPCRs to Erk1/2 signaling. However, their role in GPCR-operated Erk1/2 activation differs between GPCRs and the underlying mechanism remains poorly characterized. Here, we show that activation of serotonin 5-HT 2C receptors, which engage Erk1/2 pathway via a b-arrestin-dependent mechanism, promotes MEK-dependent b-arrestin2 phosphorylation at Thr 383 , a necessary step for Erk recruitment to the receptor/b-arrestin complex and Erk activation. Likewise, Thr 383 phosphorylation is involved in b-arrestin-dependent Erk1/2 stimulation elicited by other GPCRs such as b 2-adrenergic, FSH and CXCR4 receptors, but does not affect the b-arrestin-independent Erk1/2 activation by 5-HT 4 receptor. Collectively, these data show that b-arrestin2 phosphorylation at Thr 383 underlies b-arrestin-dependent Erk1/2 activation by GPCRs.
Fichier principal
Vignette du fichier
Cassier et al Elife 2017.pdf (3.72 Mo) Télécharger le fichier
Origine : Publication financée par une institution
Loading...

Dates et versions

hal-02365986 , version 1 (15-11-2019)

Licence

Paternité

Identifiants

Citer

Elisabeth Cassier, Nathalie Gallay, Thomas Bourquard, Sylvie Claeysen, Joël Bockaert, et al.. Phosphorylation of b-arrestin2 at Thr 383 by MEK underlies b-arrestin-dependent activation of Erk1/2 by GPCRs. eLife, 2017, 6, pp.1-21. ⟨10.7554/eLife.23777⟩. ⟨hal-02365986⟩
202 Consultations
123 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More