Location, location, deUFMylation: Coordinating ribosome quality control at the ER

IF 9 1区生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY

Cell Chemical Biology Pub Date : 2026-10-15 DOI:10.1016/j.chembiol.2026.08.015

Alexander R. Mikesell, Zachary T. Campbell

引用次数: 0

Abstract

Endoplasmic-reticulum-associated ribosome quality control (ER-RQC) requires ubiquitin-fold modifier 1 (UFM1) for UFMylation of the ribosomal protein RPL26. In the August 6 issue of Molecular Cell, Mao et al.¹ identify an ER-associated complex (UFSP2/ODR4) as critical for deUFMylation of RPL26 and uncover a critical physiologic role for UFSP2 in neuronal proteostasis.

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定位，定位，去髓化：协调急诊室核糖体质量控制

内质网相关核糖体质量控制（ER-RQC）需要泛素折叠修饰物1 （UFM1）来实现核糖体蛋白RPL26的ufmy化。在8月6日出版的《分子细胞》（Molecular Cell）杂志上，Mao等人1发现了er相关复合物（UFSP2/ODR4）对RPL26的去ufmyylation至关重要，并揭示了UFSP2在神经元蛋白酶抑制中的关键生理作用。

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

Cell Chemical Biology Biochemistry, Genetics and Molecular Biology-Molecular Medicine

CiteScore

14.70

自引率

2.30%

发文量

143

期刊介绍： Cell Chemical Biology, a Cell Press journal established in 1994 as Chemistry & Biology, focuses on publishing crucial advances in chemical biology research with broad appeal to our diverse community, spanning basic scientists to clinicians. Pioneering investigations at the chemistry-biology interface, the journal fosters collaboration between these disciplines. We encourage submissions providing significant conceptual advancements of broad interest across chemical, biological, clinical, and related fields. Particularly sought are articles utilizing chemical tools to perturb, visualize, and measure biological systems, offering unique insights into molecular mechanisms, disease biology, and therapeutics.