Evidence map›Paper›PMID 31802140›Full record

ArticleCellular and molecular life sciences : CMLS2020

Amyotrophic lateral sclerosis-linked UBQLN2 mutants inhibit endoplasmic reticulum to Golgi transport, leading to Golgi fragmentation and ER stress.

Mark Halloran, Audrey M G Ragagnin, Marta Vidal, Sonam Parakh, Shu Yang, Benjamin Heng, Natalie Grima, Hamideh Shahheydari, Kai-Ying Soo, Ian Blair and 3 more

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 40 citations in OpenAlex.

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  12. Nlp-dependent ER-to-Golgi transport.International journal of biological sciences · 2024
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  14. Cells · 2023
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  19. Serpin neuropathology in the P497S UBQLN2 mouse model of ALS/FTD.Brain pathology (Zurich, Switzerland) · 2021
    Article
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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

13 authors at 2 institutions in 1 country.

Mark HalloranDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia.
Audrey M G RagagninDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia.
Marta VidalDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia.
Sonam ParakhDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia.
Shu YangDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia.
Benjamin HengDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia.
Natalie GrimaDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia.
Hamideh ShahheydariDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia.
Kai-Ying SooDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia.
Ian BlairDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia.
Gilles J GuilleminDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia.
Vinod SundaramoorthyDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia.
Julie D AtkinDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia. julie.atkin@mq.edu.au.
Macquarie University · AULa Trobe University · AU

Funding

National Health and Medical Research Council 10305133National Health and Medical Research Council 1086887National Health and Medical Research Council 1095215
6 · The paper itself

Abstract

Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are fatal neurodegenerative diseases that are related genetically and pathologically. Mutations in the UBQLN2 gene, encoding the ubiquitin-like protein ubiquilin2, are associated with familial ALS/FTD, but the pathophysiological mechanisms remain unclear. Here, we demonstrate that ALS/FTD UBQLN2 mutants P497H and P506T inhibit protein transport from the endoplasmic reticulum (ER) to the Golgi apparatus in neuronal cells. In addition, we observed that Sec31-positive ER exit sites are clustered in UBQLN2

Indexed as

Adaptor Proteins, Signal TransducingAmyotrophic Lateral SclerosisAnimalsAutophagy-Related ProteinsCells, CulturedEndoplasmic ReticulumEndoplasmic Reticulum StressFrontotemporal DementiaGolgi ApparatusHumansMiceMutagenesis, Site-DirectedNeuronsProtein TransportAdaptor Proteins, Signal TransducingAutophagy-Related ProteinsUBQLN2 protein, humanAmyotrophic lateral sclerosisER-Golgi traffickingER stressGolgi fragmentationUbiquilin-2Unfolded protein response

Identifiers

PMID31802140
PMCPMC11105036
OpenAlexW2992540821

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.