Evidence map›Paper›PMID 39738171›Full record

ArticleNature communications2024

NS1 binding protein regulates stress granule dynamics and clearance by inhibiting p62 ubiquitination.

Pureum Jeon, Hyun-Ji Ham, Haneul Choi, Semin Park, Jae-Woo Jang, Sang-Won Park, Dong-Hyung Cho, Hyun-Jeong Lee, Hyun Kyu Song, Masaaki Komatsu and 3 more

Erratum issuedAbstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors.

Pureum Jeon *Department of Biological Sciences and Biotechnology, College of Life Sciences and Nanotechnology, Hannam University, Daejeon, Korea.ORCID 0000-0003-3929-0781
Hyun-Ji Ham *Department of Biological Sciences and Biotechnology, College of Life Sciences and Nanotechnology, Hannam University, Daejeon, Korea.ORCID 0009-0004-6691-9674
Haneul Choi *Department of Biological Sciences and Biotechnology, College of Life Sciences and Nanotechnology, Hannam University, Daejeon, Korea.ORCID 0009-0006-6629-2212
Semin ParkDepartment of Biological Sciences and Biotechnology, College of Life Sciences and Nanotechnology, Hannam University, Daejeon, Korea.
Jae-Woo JangDepartment of Biological Sciences and Biotechnology, College of Life Sciences and Nanotechnology, Hannam University, Daejeon, Korea.
Sang-Won ParkDepartment of Ecological Science, College of Ecology and Environment, Kyungpook National University, Sangju, Korea.
Dong-Hyung ChoSchool of Life Sciences, BK21 FOUR KNU Creative BioRearch Group, Kyungpook National University, Daegu, 41566, Korea.
Hyun-Jeong LeeDepartment of Life Sciences, Korea University, Seoul, Korea.ORCID 0009-0007-2670-542X
Hyun Kyu SongDepartment of Life Sciences, Korea University, Seoul, Korea.ORCID 0000-0001-5684-4059
Masaaki KomatsuDepartment of Physiology, Juntendo University Graduate School of Medicine, Bunkyo-ku, Tokyo, Japan.ORCID 0000-0001-7672-7722
Dohyun HanDepartment of Transdiciplinary Medicine, Seoul National University Hospital, Seoul, Korea.ORCID 0000-0002-0841-1598
Deok-Jin JangDepartment of Ecological Science, College of Ecology and Environment, Kyungpook National University, Sangju, Korea. jangdj@knu.ac.kr.ORCID 0000-0003-3091-4842
Jin-A LeeDepartment of Biological Sciences and Biotechnology, College of Life Sciences and Nanotechnology, Hannam University, Daejeon, Korea. leeja@hnu.kr.ORCID 0000-0002-6757-8371

Funding

Japan Agency for Medical Research and Development (AMED) JP22gm1410004h0003MEXT | Japan Society for the Promotion of Science (JSPS) 23K20044MEXT | Japan Society for the Promotion of Science (JSPS) 24H00060MEXT | Japan Society for the Promotion of Science (JSPS) JP19H05706MEXT | Japan Society for the Promotion of Science (JSPS) JP21H004771National Research Foundation of Korea (NRF) 2020M3E5D9079911National Research Foundation of Korea (NRF) 2023R1A2C2008092National Research Foundation of Korea (NRF) RS-2023-00218515
6 · The paper itself

Abstract

The NS1 binding protein, known for interacting with the influenza A virus protein, is involved in RNA processing, cancer, and nerve cell growth regulation. However, its role in stress response independent of viral infections remains unclear. This study investigates NS1 binding protein's function in regulating stress granules during oxidative stress through interactions with GABARAP subfamily proteins. We find that NS1 binding protein localizes to stress granules, interacting with core components, GABARAP proteins, and p62, a protein involved in autophagy. In cells lacking NS1 binding protein, stress granule dynamics are altered, and p62 ubiquitination is increased, suggesting impaired stress granule degradation. Overexpression of NS1 binding protein reduces p62 ubiquitination. In amyotrophic lateral sclerosis patient-derived neurons, reduced NS1 binding protein and p62 disrupt stress granule morphology. These findings identify NS1 binding protein as a negative regulator of p62 ubiquitination and a facilitator of GABARAP recruitment to stress granules, implicating it in stress granule regulation and amyotrophic lateral sclerosis pathogenesis.

Indexed as

Adaptor Proteins, Signal TransducingAmyotrophic Lateral SclerosisSequestosome-1 ProteinStress GranulesUbiquitinationApoptosis Regulatory ProteinsAutophagyCytoplasmic GranulesHEK293 CellsHeLa CellsHumansMicrotubule-Associated ProteinsNeuronsOxidative StressProtein BindingViral Nonstructural ProteinsAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsGABARAP protein, humanMicrotubule-Associated ProteinsNUB1 protein, humanSequestosome-1 ProteinSQSTM1 protein, humanViral Nonstructural Proteins

Identifiers

PMID39738171
PMCPMC11686067

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.