EMAIL THIS PAGE TO A FRIEND

Scientific reports

eIF4B phosphorylation at Ser504 links synaptic activity with protein translation in physiology and pathology.


PMID 28874824

Abstract

Neuronal physiology requires activity-driven protein translation, a process in which translation initiation factors are key players. We focus on eukaryotic initiation factor 4B (eIF4B), a regulator of protein translation, whose function in neurons is undetermined. We show that neuronal activity affects eIF4B phosphorylation and identify Ser504 as a phosphorylation site regulated by casein kinases and sensitive to the activation of metabotropic glutamate receptors. Ser504 phosphorylation increases eIF4B recruitment to the pre-initiation complex and influences eIF4B localization at synapses. Moreover, Ser504 phosphorylation modulates the translation of protein kinase Mζ. Therefore, by sensing synaptic activity, eIF4B could adjust translation to neuronal needs, promoting adaptive changes in synaptic plasticity. We also show that Ser504 phosphorylation is increased in vivo in a rat model of epilepsy during epileptogenesis i.e. when translation drives maladaptive synaptic changes. We propose eIF4B as a mediator between neuronal activity and translation, with relevance in the control of synaptic plasticity.

Related Materials

Product #

Image

Description

Molecular Formula

Add to Cart

A254
AIDA, solid
C11H11NO4
D1944
D4476, ≥98% (HPLC), solid
C23H18N4O3
N0287
NNC 55-0396 hydrate, ≥98% (HPLC)
C30H40Cl2FN3O2 · xH2O