Evidence map›Paper›PMID 32376919›Full record

ArticleScientific reports2020

Proteomics-Based Approach Identifies Altered ER Domain Properties by ALS-Linked VAPB Mutation.

Tomoyuki Yamanaka, Risa Nishiyama, Tomomi Shimogori, Nobuyuki Nukina

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. 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
1.4field-weighted citation impact, top 15% 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, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. ALS-Linked VapB P56S Mutation Alters Neuronal Mitochondrial Turnover at the Synapse.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Sequestosome 1 Is Part of the Interaction Network of VAPB.International journal of molecular sciences · 2021
    Article
  11. Article
  12. Review
  13. Review
  14. ER-PM Contact Sites - SNARING Actors in Emerging Functions.Frontiers in cell and developmental biology · 2021
    Review
  15. Article
  16. Molecular and Cellular Mechanisms Affected in ALS.Journal of personalized medicine · 2020
    Review
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

4 authors at 2 institutions in 1 country.

Tomoyuki YamanakaLaboratory of Structural Neuropathology, Doshisha University Graduate School of Brain Science, Kyoto, Japan. toyamana@mail.doshisha.ac.jp.
Risa NishiyamaLaboratory of Structural Neuropathology, Doshisha University Graduate School of Brain Science, Kyoto, Japan.
Tomomi ShimogoriMolecular Mechanisms of Brain Development, RIKEN Center for Brain Science, Saitama, 351-0198, Japan.
Nobuyuki NukinaLaboratory of Structural Neuropathology, Doshisha University Graduate School of Brain Science, Kyoto, Japan. nnukina@mail.doshisha.ac.jp.
Doshisha University · JPRIKEN Center for Brain Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An ER transmembrane protein, vesicle-associated membrane protein-associated protein B (VAPB), binds to several organelle-resident membrane proteins to mediate ER-organelle tethering. Mutation in amyotrophic lateral sclerosis (ALS) induces protein misfolding and aggregation, leading to ER disorganization. Gain or loss of function is suggested for VAPB mutation, however comprehensive study focusing on VAPB-ER domain has yet been performed. We here conducted proteomic characterization of the ER containing VAPB and its ALS-linked P56S mutant. For this purpose, we first optimized the proteomics of different ER domains immuno-isolated from cultured cells, and identified ER sheet- and tubule-specific proteomes. By using these as references, we found that VAPB-ER proteome had intermediate ER domain properties but its tubular property was specifically decreased by its mutation. Biochemical, immunofluorescence and proximity ligation assays suggested this was mediated by delocalization of VAPB from ER tubules. The VAPB-ER proteomics further suggested reduced incorporation of multiple proteins located in different organelles, which was confirmed by proximity ligation assay. Taken together, our proteomics-based approach indicates altered ER domain properties and impaired ER-organelle tethering by VAPB mutation.

Indexed as

MutationProteomicsAmyotrophic Lateral SclerosisAnimalsCell LineEndoplasmic ReticulumMiceProtein DomainsProtein Interaction MappingVesicular Transport ProteinsVAPB protein, mouseVesicular Transport Proteins

Identifiers

PMID32376919
PMCPMC7203144
OpenAlexW3023894234

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.