Deciphering the role of TYK2 in tau phosphorylation and pathology.

IF 15.1 1区医学 Q1 NEUROSCIENCES

Trends in Neurosciences Pub Date : 2025-03-01 Epub Date: 2025-02-10 DOI:10.1016/j.tins.2025.01.004

Alexander Fröhlich, Kathryn R Bowles

引用次数: 0

Abstract

Tau phosphorylation plays an essential role in regulating tau's microtubule-stabilizing function, but its hyperphosphorylation drives tauopathies such as Alzheimer's disease (AD). In a recent study, Kim and colleagues decipher that tyrosine kinase 2 (TYK2) phosphorylates tau at tyrosine 29, promoting its stabilization and aggregation by interfering with autophagic clearance, providing novel insights into tau pathology and potential therapeutic strategies.

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解读TYK2在tau磷酸化和病理中的作用。

Tau磷酸化在调节Tau的微管稳定功能中起着至关重要的作用，但其过度磷酸化会导致Tau病，如阿尔茨海默病（AD）。在最近的一项研究中，Kim和他的同事们发现酪氨酸激酶2 （TYK2）在酪氨酸29位点磷酸化tau蛋白，通过干扰自噬清除促进其稳定和聚集，为tau蛋白病理和潜在的治疗策略提供了新的见解。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Trends in Neurosciences 医学-神经科学

CiteScore

26.50

自引率

1.30%

发文量

123

审稿时长

6-12 weeks

期刊介绍： For over four decades, Trends in Neurosciences (TINS) has been a prominent source of inspiring reviews and commentaries across all disciplines of neuroscience. TINS is a monthly, peer-reviewed journal, and its articles are curated by the Editor and authored by leading researchers in their respective fields. The journal communicates exciting advances in brain research, serves as a voice for the global neuroscience community, and highlights the contribution of neuroscientific research to medicine and society.