Evidence map›Paper›PMID 42252285›Full record

ArticleCell death & disease2026

Lysine acetyltransferase 8-mediated histone acetylation, regulated by GBA1, is associated with lysosomal function related to α-Synuclein pathology.

Yifan Cao, Zhixiong Zhang, Xinbei Gu, Haifeng Lu, Jin Wu, Chuang Zhang, Xinyue Huang, Haitao Qin, Feng Liu, Zhenhua Liu and 6 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell death & disease, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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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.

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

16 authors.

Yifan CaoLaboratory of Molecular Neuropathology, Department of Pharmacology, Jiangsu Key Laboratory of Drug Discovery and Translational Research for Brain Diseases, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, China.
Zhixiong ZhangLaboratory of Molecular Neuropathology, Department of Pharmacology, Jiangsu Key Laboratory of Drug Discovery and Translational Research for Brain Diseases, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, China.
Xinbei GuLaboratory of Molecular Neuropathology, Department of Pharmacology, Jiangsu Key Laboratory of Drug Discovery and Translational Research for Brain Diseases, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, China.
Haifeng LuDepartment of Neurology, the First Affiliated Hospital of Soochow University, Suzhou, Jiangsu, China.
Jin WuLaboratory of Molecular Neuropathology, Department of Pharmacology, Jiangsu Key Laboratory of Drug Discovery and Translational Research for Brain Diseases, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, China.
Chuang ZhangLaboratory of Molecular Neuropathology, Department of Pharmacology, Jiangsu Key Laboratory of Drug Discovery and Translational Research for Brain Diseases, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, China.
Xinyue HuangLaboratory of Molecular Neuropathology, Department of Pharmacology, Jiangsu Key Laboratory of Drug Discovery and Translational Research for Brain Diseases, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, China.
Haitao QinJiangsu Key Laboratory of Translational Research and Therapy for Neuro-Psycho-Diseases and Department of Medicinal Chemistry, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, China.
Feng LiuJiangsu Key Laboratory of Translational Research and Therapy for Neuro-Psycho-Diseases and Department of Medicinal Chemistry, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, China.
Zhenhua LiuDepartment of Neurology & National Clinical Research Centre for Geriatric Disorders, Xiangya Hospital, Central South University, Changsha, Hunan, China.
Beisha TangDepartment of Neurology & National Clinical Research Centre for Geriatric Disorders, Xiangya Hospital, Central South University, Changsha, Hunan, China.ORCID http://orcid.org/0000-0003-2120-1576
Xiaojun LuSuzhou Key Laboratory of Geriatric Neurological Disorders, Department of Neurosurgery, the First People's Hospital of Taicang, Taicang Affiliated Hospital of Soochow University, Suzhou, Jiangsu, China.
Haigang RenLaboratory of Molecular Neuropathology, Department of Pharmacology, Jiangsu Key Laboratory of Drug Discovery and Translational Research for Brain Diseases, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, China.ORCID http://orcid.org/0000-0001-8844-4754
Hongyang SunLaboratory of Molecular Neuropathology, Department of Pharmacology, Jiangsu Key Laboratory of Drug Discovery and Translational Research for Brain Diseases, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, China. hysun@suda.edu.cn.
Rui WangLaboratory of Molecular Neuropathology, Department of Pharmacology, Jiangsu Key Laboratory of Drug Discovery and Translational Research for Brain Diseases, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, China. rwang0828@suda.edu.cn.ORCID http://orcid.org/0000-0001-8346-5783
Guanghui WangLaboratory of Molecular Neuropathology, Department of Pharmacology, Jiangsu Key Laboratory of Drug Discovery and Translational Research for Brain Diseases, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, China. wanggh@suda.edu.cn.ORCID http://orcid.org/0000-0001-8551-6468

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysosomal defects are closely linked to Parkinson's disease (PD). Mutations in the GBA1 gene, encoding the lysosomal enzyme glucocerebrosidase (GCase), are major genetic risk factors for PD. GBA1 deficiency causes lysosomal dysfunction, leading to α-synuclein (α-syn) accumulation and PD progression. However, the underlying mechanisms remain unclear. In this study, we identified a novel GBA1-KAT8 regulatory pathway that controls lysosomal activity. GBA1 overexpression enhances lysosomal enzyme expression, regulates histone H4 acetylation at K16 via KAT8, and promotes lysosome-associated gene expression, highlighting an epigenetic mechanism in lysosomal biogenesis. Furthermore, GBA1 upregulated KAT8 expression, increased lysosomal enzyme levels, and decreased PFF-induced α-syn accumulation both in vitro and in vivo. The involvement of KAT8 as a critical acetyltransferase that modulates nuclear-lysosomal signaling pathways provides a mechanistic explanation for GBA1 deficiency-induced lysosomal dysfunction in association with PD pathology.

Indexed as

alpha-SynucleinGlucosylceramidaseHistone AcetyltransferasesHistonesLysosomesAcetylationAnimalsHumansMiceParkinson DiseaseSignal Transductionalpha-SynucleinGBA protein, humanGlucosylceramidaseHistone AcetyltransferasesHistones

Identifiers

PMID42252285
PMCPMC13462883

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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.