SQSTM1/p62 UFMylation Enhances Autophagic Clearance of Pathogenic Mutant Huntingtin

International Journal of Biological Sciences 2026 Open access

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Authors: Xiaohui Wang, Xiaowei Lv, Honglv Jiang, Wenyun Zhu, Lindong Cao, Liang Zhou, Fang Chen Lin, Rong Deng, Li‐Fang Hu, Jingjing Ma, Jia-Bin Li, Guoqiang Xu
DOI: 10.7150/ijbs.127110
Cited by: 1

Abstract

) restores the p62-mediated pathogenic autophagic degradation in primary cortical neurons and Huntington's disease mouse striatum. Mechanistically, p62 UFMylation enhances its interaction with LC3, augments autophagic flux, and eliminates pathogenic mutant huntingtin. Collectively, this work discovers a new post-translational modification, UFMylation, on p62 and establishes this modification as a key regulator of autophagy that promotes the clearance of mutant huntingtin, offering a potential target for therapeutic intervention.

Fields of Study & Subjects

Autophagy in Disease and Therapy Cellular transport and secretion Hereditary Neurological Disorders

Publication details

Journal / source
International Journal of Biological Sciences
Publisher
Ivyspring International Publisher
Volume
22
Issue
10
Pages
5475–5494
Publication date
18 May 2026
Language
EN