Evidence map›Paper›PMID 40483356›Full record

ArticleNPJ Parkinson's disease2025

EGFR phosphorylates DNAJB1 to suppress α-synuclein aggregation in Parkinson's disease.

Yun-Yu Huang, Sue-Jane Lin, Wei-Yu Chiang, Yuan-Teng Chang, Chan-Chih Yang, Chia-Yu Liao, Ya-Lan Chang, Chin-Hsien Lin, Shu-Chun Teng

Abstract read
In one paragraph

Article in NPJ Parkinson's disease, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed, 1 pooled it
–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

5 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Article
  4. DnaJB1 chaperone inhibits tau aggregation by recognizing its N-terminus.bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
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.

Yun-Yu HuangDepartment of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Sue-Jane LinDepartment of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Wei-Yu ChiangDepartment of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Yuan-Teng ChangDepartment of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Chan-Chih YangDepartment of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Chia-Yu LiaoDepartment of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Ya-Lan ChangDepartment of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Chin-Hsien LinDepartment of Neurology, National Taiwan University Hospital Taipei, Taipei, Taiwan. chlin@ntu.edu.tw.
Shu-Chun TengDepartment of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan. shuchunteng@ntu.edu.tw.

Funding

National Health Research Institutes NHRI-EX113-11136NINational Science and Technology Council in Taiwan 112-2311-B-002 -015 -MY3
6 · The paper itself

Abstract

Parkinson's disease (PD), characterized by α-synuclein accumulation in dopaminergic neurons, is a common neurodegenerative disorder. Recent findings highlight DNAJB1 as a crucial factor in the disaggregation of α-synuclein fibrils in vitro, yet the underlying mechanisms and regulatory processes in neuronal cells remain largely undefined. This study reveals that DNAJB1 facilitates the clearance of α-synuclein via the Hsp70 chaperone system. Phosphorylation of DNAJB1 at tyrosine 5 by the epidermal growth factor receptor (EGFR) is essential for mitigating α-synuclein aggregation, enhancing its interaction with Hsp70. Dysregulation of this pathway disrupts α-synuclein delivery to Hsp70, worsening aggregation in neuronal cells. Analysis of human brain lysates from individuals with PD and unaffected controls showed reduced levels of EGFR and DNAJB1, with an increase in phosphorylated DNAJB1 at Y5. These findings elucidate mechanisms in PD pathology and suggest DNAJB1 as a promising candidate for targeted therapeutic strategies.

Identifiers

PMID40483356
PMCPMC12145416

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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.