Evidence map›Paper›PMID 39035418›Full record

ArticleBrain communications2024

Spatial selectivity of ATase inhibition in mouse models of Charcot-Marie-Tooth disease.

Gonzalo Fernandez-Fuente, Mark A Farrugia, Yajing Peng, Andrew Schneider, John Svaren, Luigi Puglielli

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Brain communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

6 authors.

Gonzalo Fernandez-FuenteDepartment of Medicine, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI 53705, USA.
Mark A FarrugiaDepartment of Medicine, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI 53705, USA.
Yajing PengDepartment of Medicine, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI 53705, USA.
Andrew SchneiderWaisman Center, University of Wisconsin-Madison, Madison, WI 53705, USA.
John SvarenWaisman Center, University of Wisconsin-Madison, Madison, WI 53705, USA.ORCID https://orcid.org/0000-0003-2963-7921
Luigi PuglielliDepartment of Medicine, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI 53705, USA.ORCID https://orcid.org/0000-0003-0259-8424

Funding

Waisman Center Intellectual and Developmental Disabilities Research CenterP50HD105353 · NICHD · UNIVERSITY OF WISCONSIN-MADISON · PI Brittany Gail Travers · 2021 to 2026
$8.5M
Spastic paraplegia, neurodegeneration and autism: possible role for AT- 1/SLC33A1?R01NS094154 · NINDS · UNIVERSITY OF WISCONSIN-MADISON · PI Luigi Puglielli · 2015 to 2026
$4.3M
Creating a region- specific biomolecular atlas of the brain of Alzheimer’s diseaseR01AG078794 · NIA · UNIVERSITY OF WISCONSIN-MADISON · PI LINGJUN LI, Luigi Puglielli · 2022 to 2026
$3.7M
Schwann Cell Reprogramming after Nerve InjuryR01NS130566 · NINDS · UNIVERSITY OF WISCONSIN-MADISON · PI Rajeshwar B Awatramani, John P Svaren · 2023 to 2026
$2.0M
ATase1 and ATase2, proteostasis, and neurological diseasesR01GM148487 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Luigi Puglielli · 2023 to 2026
$1.2M
NIA NIH HHS R01 AG078794NICHD NIH HHS P50 HD105353NIGMS NIH HHS R01 GM148487NINDS NIH HHS R01 NS094154NINDS NIH HHS R01 NS130566
6 · The paper itself

Abstract

The endoplasmic reticulum acetylation machinery has emerged as a new branch of the larger endoplasmic reticulum quality control system. It regulates the selection of correctly folded polypeptides as well as reticulophagy-mediated removal of toxic protein aggregates with the former being a particularly important aspect of the proteostatic functions of endoplasmic reticulum acetylation. Essential to this function is the Nε-lysine acetyltransferase activity of acetyltransferase 1 and acetyltransferase 2, which regulates the induction of endoplasmic reticulum-specific autophagy through the acetylation of the autophagy-related protein 9A. Here, we used three mouse models of Charcot-Marie-Tooth disease, peripheral myelin protein 22/Tr-J, C3-peripheral myelin protein 22 and myelin protein zero/ttrr, to study spatial and translational selectivity of endoplasmic reticulum acetyltransferase inhibitors. The results show that inhibition of the endoplasmic reticulum acetyltransferases selectively targets misfolding/pro-aggregating events occurring in the lumen of the organelle. Therefore, they establish acetyltransferase 1 and acetyltransferase 2 as the first proven targets for disease-causing proteotoxic states that initiate within the lumen of the endoplasmic reticulum/secretory pathway.

Indexed as

acetylationATaseCharcot–Marie–Tooth diseaseendoplasmic reticulumproteostasis

Identifiers

PMID39035418
PMCPMC11258571

What OpenQuestion holds

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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.