Evidence map›Paper›PMID 38617306›Full record

ArticlebioRxiv : the preprint server for biology2024

A mechanism that transduces lysosomal damage signals to stress granule formation for cell survival.

Jacob Duran, Suttinee Poolsup, Lee Allers, Monica Rosas Lemus, Qiuying Cheng, Jing Pu, Michelle Salemi, Brett Phinney, Jingyue Jia

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

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

9 authors at 1 institution in 1 country.

Jacob DuranCenter for Global Health, Department of Internal Medicine, University of New Mexico Health Sciences Center, Albuquerque, NM 87106, USA.
Suttinee PoolsupCenter for Global Health, Department of Internal Medicine, University of New Mexico Health Sciences Center, Albuquerque, NM 87106, USA.
Lee AllersAutophagy, Inflammation and Metabolism Center of Biochemical Research Excellence, Albuquerque, NM 87106, USA.
Monica Rosas LemusAutophagy, Inflammation and Metabolism Center of Biochemical Research Excellence, Albuquerque, NM 87106, USA.
Qiuying ChengCenter for Global Health, Department of Internal Medicine, University of New Mexico Health Sciences Center, Albuquerque, NM 87106, USA.
Jing PuDepartment of Molecular Genetics and Microbiology, University of New Mexico Health Sciences Center, Albuquerque, NM 87106, USA.
Michelle SalemiProteomics Core Facility, University of California Davis Genome Center, University of California, Davis, CA 95616, USA.
Brett PhinneyProteomics Core Facility, University of California Davis Genome Center, University of California, Davis, CA 95616, USA.
Jingyue JiaCenter for Global Health, Department of Internal Medicine, University of New Mexico Health Sciences Center, Albuquerque, NM 87106, USA.ORCID 0000-0002-1522-9612
University of New Mexico · US

Funding

Unfolded Protein Response and Autophagy in T Helper Cell Effector FunctionP20GM121176 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI Samuel Joseph Endicott · 2017 to 2026
$24.9M
Phinney - Orbitrap Fusion ETDS10OD021801 · OD · UNIVERSITY OF CALIFORNIA AT DAVIS · PI PHINNEY, BRETT S · 2016 to 2016
$600k
QE-HF-X Mass SpectrometerS10OD026918 · OD · UNIVERSITY OF CALIFORNIA AT DAVIS · PI PHINNEY, BRETT S · 2020 to 2020
$600k
NIGMS NIH HHS P20 GM121176NIH HHS S10 OD021801NIH HHS S10 OD026918
6 · The paper itself

Abstract

Lysosomal damage poses a significant threat to cell survival. Our previous work has reported that lysosomal damage induces stress granule (SG) formation. However, the importance of SG formation in determining cell fate and the precise mechanisms through which lysosomal damage triggers SG formation remains unclear. Here, we show that SG formation is initiated via a novel calcium-dependent pathway and plays a protective role in promoting cell survival in response to lysosomal damage. Mechanistically, we demonstrate that during lysosomal damage, ALIX, a calcium-activated protein, transduces lysosomal damage signals by sensing calcium leakage to induce SG formation by controlling the phosphorylation of eIF2α. ALIX modulates eIF2α phosphorylation by regulating the association between PKR and its activator PACT, with galectin-3 exerting a negative effect on this process. We also found this regulatory event of SG formation occur on damaged lysosomes. Collectively, these investigations reveal novel insights into the precise regulation of SG formation triggered by lysosomal damage, and shed light on the interaction between damaged lysosomes and SGs. Importantly, SG formation is significant for promoting cell survival in the physiological context of lysosomal damage inflicted by SARS-CoV-2 ORF3a, adenovirus infection, Malaria hemozoin, proteopathic tau as well as environmental hazard silica.

Identifiers

PMID38617306
PMCPMC11014484
OpenAlexW4393339918

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.