Synaptic FUS accumulation triggers early misregulation of synaptic RNAs in a mouse model of ALS

Mutations in the RNA-binding protein FUS contribute to ALS. Here the authors use CLIP-seq on synaptoneurosomes to identify proteins associated with synapse organization and plasticity that are differentially regulated in a knock-in ALS mouse model.

Bibliographic Details
Main Authors: Sonu Sahadevan, Katharina M. Hembach, Elena Tantardini, Manuela Pérez-Berlanga, Marian Hruska-Plochan, Salim Megat, Julien Weber, Petra Schwarz, Luc Dupuis, Mark D. Robinson, Pierre De Rossi, Magdalini Polymenidou
Format: Article
Language:English
Published: Nature Publishing Group 2021-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-23188-8
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spelling doaj-e9c043534e61495b8e1dfb249245ca1e2021-05-23T11:12:57ZengNature Publishing GroupNature Communications2041-17232021-05-0112111710.1038/s41467-021-23188-8Synaptic FUS accumulation triggers early misregulation of synaptic RNAs in a mouse model of ALSSonu Sahadevan0Katharina M. Hembach1Elena Tantardini2Manuela Pérez-Berlanga3Marian Hruska-Plochan4Salim Megat5Julien Weber6Petra Schwarz7Luc Dupuis8Mark D. Robinson9Pierre De Rossi10Magdalini Polymenidou11Department of Quantitative Biomedicine, University of ZurichDepartment of Quantitative Biomedicine, University of ZurichDepartment of Quantitative Biomedicine, University of ZurichDepartment of Quantitative Biomedicine, University of ZurichDepartment of Quantitative Biomedicine, University of ZurichInserm, University of StrasbourgDepartment of Quantitative Biomedicine, University of ZurichInstitute of Neuropathology, University Hospital ZurichInserm, University of StrasbourgDepartment of Molecular Life Sciences and SIB Swiss Institute of Bioinformatics, University of ZurichDepartment of Quantitative Biomedicine, University of ZurichDepartment of Quantitative Biomedicine, University of ZurichMutations in the RNA-binding protein FUS contribute to ALS. Here the authors use CLIP-seq on synaptoneurosomes to identify proteins associated with synapse organization and plasticity that are differentially regulated in a knock-in ALS mouse model.https://doi.org/10.1038/s41467-021-23188-8
collection DOAJ
language English
format Article
sources DOAJ
author Sonu Sahadevan
Katharina M. Hembach
Elena Tantardini
Manuela Pérez-Berlanga
Marian Hruska-Plochan
Salim Megat
Julien Weber
Petra Schwarz
Luc Dupuis
Mark D. Robinson
Pierre De Rossi
Magdalini Polymenidou
spellingShingle Sonu Sahadevan
Katharina M. Hembach
Elena Tantardini
Manuela Pérez-Berlanga
Marian Hruska-Plochan
Salim Megat
Julien Weber
Petra Schwarz
Luc Dupuis
Mark D. Robinson
Pierre De Rossi
Magdalini Polymenidou
Synaptic FUS accumulation triggers early misregulation of synaptic RNAs in a mouse model of ALS
Nature Communications
author_facet Sonu Sahadevan
Katharina M. Hembach
Elena Tantardini
Manuela Pérez-Berlanga
Marian Hruska-Plochan
Salim Megat
Julien Weber
Petra Schwarz
Luc Dupuis
Mark D. Robinson
Pierre De Rossi
Magdalini Polymenidou
author_sort Sonu Sahadevan
title Synaptic FUS accumulation triggers early misregulation of synaptic RNAs in a mouse model of ALS
title_short Synaptic FUS accumulation triggers early misregulation of synaptic RNAs in a mouse model of ALS
title_full Synaptic FUS accumulation triggers early misregulation of synaptic RNAs in a mouse model of ALS
title_fullStr Synaptic FUS accumulation triggers early misregulation of synaptic RNAs in a mouse model of ALS
title_full_unstemmed Synaptic FUS accumulation triggers early misregulation of synaptic RNAs in a mouse model of ALS
title_sort synaptic fus accumulation triggers early misregulation of synaptic rnas in a mouse model of als
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-05-01
description Mutations in the RNA-binding protein FUS contribute to ALS. Here the authors use CLIP-seq on synaptoneurosomes to identify proteins associated with synapse organization and plasticity that are differentially regulated in a knock-in ALS mouse model.
url https://doi.org/10.1038/s41467-021-23188-8
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