Evidence map›Paper›PMID 42816892›Full record

ReviewTranslational neurodegeneration2026

Fyn kinase: a key mechanistic regulator and therapeutic target in tauopathy and neurodegenerative diseases.

Haiwen Wang, Xing Fan, Jianchao Ping, Qian Shao, Cai Wang, Hao Wang, Qiuhong Ji, Min Su, Wei Qian

Abstract readReview
In one paragraph

Review in Translational neurodegeneration, 2026. 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.

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.

Haiwen Wang *Department of Biochemistry and Molecular Biology, School of Medicine, Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, 226001, China.
Xing Fan *Department of Biochemistry and Molecular Biology, School of Medicine, Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, 226001, China.
Jianchao PingDepartment of Biochemistry and Molecular Biology, School of Medicine, Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, 226001, China.
Qian ShaoDepartment of Biochemistry and Molecular Biology, School of Medicine, Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, 226001, China.
Cai WangDepartment of Biochemistry and Molecular Biology, School of Medicine, Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, 226001, China.
Hao WangDepartment of Biochemistry and Molecular Biology, School of Medicine, Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, 226001, China.
Qiuhong JiAffiliated Hospital of Nantong University, Nantong, 226001, China. jiqiuhong@ntu.edu.cn.
Min SuAffiliated Hospital of Nantong University, Nantong, 226001, China. sumin_nt@126.com.
Wei QianDepartment of Biochemistry and Molecular Biology, School of Medicine, Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, 226001, China. weiqian@ntu.edu.cn.

Funding

Nantong Natural Science Foundation JC2023042National Natural Science Foundation of China 82473926National Natural Science Foundation of China 82607575
6 · The paper itself

Abstract

Synaptic dysfunction and intracellular accumulation of pathological tau are convergent hallmarks of Alzheimer's disease (AD) and related tauopathies, yet the molecular mechanisms coupling these events to widespread neurodegeneration remain incompletely understood. The Src family kinase Fyn has emerged as a critical signaling hub that integrates upstream pathogenic triggers, such as amyloid-β (Aβ), with downstream neurotoxic cascades. Here, we review the multifaceted roles of Fyn in orchestrating synaptic failure, highlighting how Fyn recruitment by mislocalized tau promotes N-methyl-D-aspartate receptor hyperactivation and calcium dysregulation. We examine the biophysical basis of Fyn-tau interactions, particularly the role of liquid-liquid phase separation in stabilizing toxic signaling complexes. We also discuss how aberrant Fyn signaling in microglia and astrocytes amplifies neuroinflammation. Finally, we evaluate the potential of Fyn as a therapeutic target, emphasizing the necessity of strategies that selectively uncouple pathological signaling from physiological functions to effectively halt disease progression.

Indexed as

Neurodegenerative DiseasesProto-Oncogene Proteins c-fynTauopathiesAnimalsHumansSignal Transductiontau ProteinsFYN protein, humanProto-Oncogene Proteins c-fyntau ProteinsFyn kinaseNeurodegenerative diseasesNeurotransmittersSrc family kinasesTauopathy

Identifiers

PMID42816892
PMCPMC13629038

What Socratic holds

Textmetadata
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 Socratic graph.