Article
The UFSP2-ODR4 complex spatially confines and dynamically controls UFM1 deconjugation to safeguard neuronal proteostasis.
Molecular cell - 6 Aug 2026
Mao Gaoxin, Ito Sota, Ishimura Ryosuke, Sakamaki Jun-Ichi, Sasaki Ryohei, Uemura Takefumi, Ishikawa Kei-Ichi, Komatsu-Hirota Satoko, Akamatsu Wado, Abe Manabu, Waguri Satoshi, Bijarnia-Mahay Sunita, Noda Nobuo N, Inada Toshifumi, Komatsu Masaaki
Abstract excerpt
The ubiquitin-fold modifier 1 (UFM1) pathway is essential for endoplasmic-reticulum-associated ribosome quality control (ER-RQC) through UFMylation of the 60S ribosomal protein RPL26, but the regulation and physiological significance of UFM1 deconjugation remain poorly understood. Here, we identify the ER-anchored UFSP2-ODR4 complex as a spatially confined deUFMylation module critical for neuronal proteostasis....
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