Language

English

Publication Date

10-4-2023

Journal

Neuron

DOI

10.1016/j.neuron.2023.06.017

PMID

37473758

PMCID

PMC10592416

PubMedCentral® Posted Date

10-4-2024

PubMedCentral® Full Text Version

Author MSS

Abstract

Dysregulation of protein synthesis is one of the key mechanisms underlying autism spectrum disorder (ASD). However, the role of a major pathway controlling protein synthesis, the integrated stress response (ISR), in ASD remains poorly understood. Here, we demonstrate that the main arm of the ISR, eIF2α phosphorylation (p-eIF2α), is suppressed in excitatory but not inhibitory neurons in a mouse model of fragile X syndrome (FXS; Fmr1−/y). We further show that the decrease in p-eIF2α is mediated via activation of the mTORC1. Genetic reduction of p-eIF2α only in excitatory neurons is sufficient to increase general protein synthesis and cause autism-like behavior. In Fmr1−/y mice, restoration of p-eIF2α solely in excitatory neurons reverses elevated protein synthesis and rescues autism-related phenotypes. Thus, we reveal a previously unknown causal relationship between excitatory neuron-specific translational control via the ISR pathway, general protein synthesis and core phenotypes reminiscent of autism in a mouse model of FXS.

Keywords

Animals, Mice, Fragile X Syndrome, Autistic Disorder, Fragile X Messenger Ribonucleoprotein 1, Autism Spectrum Disorder, Neurons, Phenotype, Mice, Knockout, Disease Models, Animal, mRNA translation, integrated stress response, autism, fragile X syndrome

Published Open-Access

yes

Included in

Neurosciences Commons

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