Evidence map›Paper›PMID 37306101›Full record

ArticleThe EMBO journal2023

Phosphorylation of phase-separated p62 bodies by ULK1 activates a redox-independent stress response.

Ryo Ikeda, Daisuke Noshiro, Hideaki Morishita, Shuhei Takada, Shun Kageyama, Yuko Fujioka, Tomoko Funakoshi, Satoko Komatsu-Hirota, Ritsuko Arai, Elena Ryzhii and 10 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
10.3field-weighted citation impact, top 1% 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

31 citing papers in PubMed, 67 citations in OpenAlex.

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  11. Mechanisms of Xuefu Zhuyu decoction in treating diabetic kidney disease-induced renal fibrosis: UPLC-Q/TOF-MS, network pharmacology, and experimental validation.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2025
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  16. Phase separation in mitochondrial fate and mitochondrial diseases.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

20 authors at 6 institutions in 2 countries.

Ryo IkedaDepartment of Physiology, Juntendo University Graduate School of Medicine, Tokyo, Japan.
Daisuke NoshiroInstitute for Genetic Medicine, Hokkaido University, Sapporo, Japan.ORCID 0000-0001-7024-2054
Hideaki MorishitaDepartment of Physiology, Juntendo University Graduate School of Medicine, Tokyo, Japan.ORCID 0000-0003-0860-8371
Shuhei TakadaDepartment of Physiology, Juntendo University Graduate School of Medicine, Tokyo, Japan.
Shun KageyamaDepartment of Physiology, Juntendo University Graduate School of Medicine, Tokyo, Japan.
Yuko FujiokaInstitute for Genetic Medicine, Hokkaido University, Sapporo, Japan.ORCID 0000-0002-6905-0669
Tomoko FunakoshiDepartment of Physiology, Juntendo University Graduate School of Medicine, Tokyo, Japan.
Satoko Komatsu-HirotaDepartment of Physiology, Juntendo University Graduate School of Medicine, Tokyo, Japan.
Ritsuko AraiDepartment of Anatomy and Histology, Fukushima Medical University School of Medicine, Fukushima, Japan.
Elena RyzhiiDepartment of Anatomy and Histology, Fukushima Medical University School of Medicine, Fukushima, Japan.ORCID 0000-0002-7794-4347
Manabu AbeDepartment of Animal Model Development, Brain Research Institute, Niigata University, Niigata, Japan.
Tomoaki KogaDepartment of Medical Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, Japan.ORCID 0000-0001-9584-2611
Hozumi MotohashiDepartment of Gene Expression Regulation, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan.
Mitsuyoshi NakaoDepartment of Medical Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, Japan.ORCID 0000-0002-2196-8673
Kenji SakimuraDepartment of Animal Model Development, Brain Research Institute, Niigata University, Niigata, Japan.
Arata HoriiDepartment of Otolaryngology Head and Neck Surgery, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.ORCID 0000-0002-6036-0492
Satoshi WaguriDepartment of Anatomy and Histology, Fukushima Medical University School of Medicine, Fukushima, Japan.ORCID 0000-0001-9919-7111
Yoshinobu IchimuraDepartment of Physiology, Juntendo University Graduate School of Medicine, Tokyo, Japan.ORCID 0000-0003-0270-7766
Nobuo N NodaInstitute for Genetic Medicine, Hokkaido University, Sapporo, Japan.ORCID 0000-0002-6940-8069
Masaaki KomatsuDepartment of Physiology, Juntendo University Graduate School of Medicine, Tokyo, Japan.ORCID 0000-0001-7672-7722
Juntendo University · JPFukushima Medical University · JPHokkaido University · JPNiigata University · JPKumamoto University · JPTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NRF2 is a transcription factor responsible for antioxidant stress responses that is usually regulated in a redox-dependent manner. p62 bodies formed by liquid-liquid phase separation contain Ser349-phosphorylated p62, which participates in the redox-independent activation of NRF2. However, the regulatory mechanism and physiological significance of p62 phosphorylation remain unclear. Here, we identify ULK1 as a kinase responsible for the phosphorylation of p62. ULK1 colocalizes with p62 bodies, directly interacting with p62. ULK1-dependent phosphorylation of p62 allows KEAP1 to be retained within p62 bodies, thus activating NRF2. p62

Indexed as

NF-E2-Related Factor 2Oxidative StressAnimalsAutophagyAutophagy-Related Protein-1 HomologHumansIntracellular Signaling Peptides and ProteinsKelch-Like ECH-Associated Protein 1MiceOxidation-ReductionPhosphorylationSequestosome-1 ProteinAutophagy-Related Protein-1 HomologIntracellular Signaling Peptides and ProteinsKelch-Like ECH-Associated Protein 1NF-E2-Related Factor 2Sequestosome-1 ProteinULK1 protein, humanKEAP1liquid-liquid phase separationNRF2/NFE2L2p62/SQSTM1ULK1

Identifiers

PMID37306101
PMCPMC10350833
OpenAlexW4380291731

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.