SHMT2 deficiency disrupts transcriptional regulation through homocysteine-mediated suppression of histone lactylation in Huntington's disease models

SHMT2 缺陷通过同型半胱氨酸介导的组蛋白乳酸化抑制作用破坏亨廷顿病模型中的转录调控

阅读:2

Abstract

Huntington's disease (HD) is a fatal neurodegenerative disorder characterized by progressive motor dysfunction, cognitive decline, and striatal neuron degeneration, primarily affecting medium spiny neurons (MSNs). Despite extensive research, the underlying metabolic vulnerabilities contributing to HD pathogenesis remain poorly understood. In this study, we employed RNA-seq and metabolomics analyses to identify marked dysregulation of 1-carbon metabolism in HD. We validated that SHMT2, a key mitochondrial enzyme in the mitochondrial 1-carbon pathway, was substantially downregulated in HD patient-derived iPSC-differentiated human striatal organoids (hSOs) and YAC128 mice. Functionally, pharmacologic inhibition or genetic deletion of SHMT2 exacerbated mutant huntingtin aggregation, induced MSN degeneration in hSOs, and impaired motor function in WT mice. Conversely, SHMT2 overexpression attenuated MSN degeneration in HD-hSOs and improved motor performance in YAC128 mice. Mechanistically, SHMT2 deficiency led to accumulation of homocysteine, which interacted with AARS1 and suppressed histone lactylation, thereby perturbing transcriptional regulation and associating with neurodegenerative phenotypes. Finally, we demonstrated that the HD clinical drug haloperidol modulated SHMT2 expression and restored histone lactylation, providing a pharmacologic tool to probe SHMT2-dependent metabolic and epigenetic regulation in HD models. These findings highlight a metabolic-epigenetic axis as a promising therapeutic target for HD.

特别声明

1、本页面内容包含部分的内容是基于公开信息的合理引用;引用内容仅为补充信息,不代表本站立场。

2、若认为本页面引用内容涉及侵权,请及时与本站联系,我们将第一时间处理。

3、其他媒体/个人如需使用本页面原创内容,需注明“来源:[生知库]”并获得授权;使用引用内容的,需自行联系原作者获得许可。

4、投稿及合作请联系:info@biocloudy.com。