Evidence map›Paper›PMID 26598648›Full record

ArticleMolecular & cellular proteomics : MCP2016

Proteomic Analysis of Dynein-Interacting Proteins in Amyotrophic Lateral Sclerosis Synaptosomes Reveals Alterations in the RNA-Binding Protein Staufen1.

Noga Gershoni-Emek, Arnon Mazza, Michael Chein, Tal Gradus-Pery, Xin Xiang, Ka Wan Li, Roded Sharan, Eran Perlson

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.2field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
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  6. Epitranscriptomic regulation by mJournal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2020
    Review
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  10. Review
  11. Review
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  13. The cytoplasmic dynein transport machinery and its many cargoes.Nature reviews. Molecular cell biology · 2018
    Review
  14. Article
  15. Article
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 3 countries.

Noga Gershoni-EmekFrom the ‡Sagol School of Neuroscience and Department of Physiology and Pharmacology, Sackler School of Medicine and.
Arnon Mazza§Blavatnik School of Computer Science, Tel Aviv University, Israel;
Michael CheinFrom the ‡Sagol School of Neuroscience and Department of Physiology and Pharmacology, Sackler School of Medicine and.
Tal Gradus-PeryFrom the ‡Sagol School of Neuroscience and Department of Physiology and Pharmacology, Sackler School of Medicine and.
Xin Xiang¶Department of Biochemistry and Molecular Biology, the Uniformed Services University of Health Sciences, Bethesda, MD;
Ka Wan Li‖Department of Molecular and Cellular Neurobiology, Center for Neurogenomics and Cognitive Research, Neuroscience Campus Amsterdam, VU University, Amsterdam, the Netherlands.
Roded Sharan§Blavatnik School of Computer Science, Tel Aviv University, Israel;
Eran PerlsonFrom the ‡Sagol School of Neuroscience and Department of Physiology and Pharmacology, Sackler School of Medicine and eranpe@post.tau.ac.il.
Tel Aviv University · ILAmsterdam Neuroscience · NLUniversity of Health Sciences

Funding

Dissecting the interaction between dynein and early endosomesR01GM097580 · NIGMS · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI XIANG, XIN · 2011 to 2014
$1.2M
NIGMS NIH HHS R01 GM097580
6 · The paper itself

Abstract

Synapse disruption takes place in many neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS). However, the mechanistic understanding of this process is still limited. We set out to study a possible role for dynein in synapse integrity. Cytoplasmic dynein is a multisubunit intracellular molecule responsible for diverse cellular functions, including long-distance transport of vesicles, organelles, and signaling factors toward the cell center. A less well-characterized role dynein may play is the spatial clustering and anchoring of various factors including mRNAs in distinct cellular domains such as the neuronal synapse. Here, in order to gain insight into dynein functions in synapse integrity and disruption, we performed a screen for novel dynein interactors at the synapse. Dynein immunoprecipitation from synaptic fractions of the ALS model mSOD1(G93A) and wild-type controls, followed by mass spectrometry analysis on synaptic fractions of the ALS model mSOD1(G93A) and wild-type controls, was performed. Using advanced network analysis, we identified Staufen1, an RNA-binding protein required for the transport and localization of neuronal RNAs, as a major mediator of dynein interactions via its interaction with protein phosphatase 1-beta (PP1B). Both in vitro and in vivo validation assays demonstrate the interactions of Staufen1 and PP1B with dynein, and their colocalization with synaptic markers was altered as a result of two separate ALS-linked mutations: mSOD1(G93A) and TDP43(A315T). Taken together, we suggest a model in which dynein's interaction with Staufen1 regulates mRNA localization along the axon and the synapses, and alterations in this process may correlate with synapse disruption and ALS toxicity.

Indexed as

ProteomicsAmyotrophic Lateral SclerosisAnimalsAxonsCytoplasmic DyneinsDisease Models, AnimalHumansMiceMotor NeuronsMutationRNA-Binding ProteinsSynapsesSynaptosomesCytoplasmic DyneinsRNA-Binding ProteinsStau1 protein, mouse

Identifiers

PMID26598648
PMCPMC4739670
OpenAlexW2173213337

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.