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作 者:Ru-na Wang Lin Li Jun Zhou Jie Ran
机构地区:[1]Center for Cell Structure and Function,Shandong Provincial Key Laboratory of Animal Resistance Biology,College of Life Sciences,Shandong Normal University,Jinan,250014,China [2]Department of Genetics and Cell Biology,College of Life Sciences,State Key Laboratory of Medicinal Chemical Biology,Haihe Laboratory of Cell Ecosystem,Nankai University,Tianjin,300071,China
出 处:《Acta Pharmacologica Sinica》2025年第4期805-815,共11页中国药理学报(英文版)
基 金:supported by grants from the National Natural Science Foundation of China(32241014 and 32170687).
摘 要:Ubiquitin fold modifier 1(UFM1)is a newly identified post-translational modifier that is involved in the UFMylation process.Similar to ubiquitination,UFMylation enables the conjugation of UFM1 to specific target proteins,thus altering their stability,activity,or localization.UFM1 chains have the potential to undergo cleavage from their associated proteins via UFM1-specific proteases,thus highlighting a reversible feature of UFMylation.This modification is conserved across nearly all eukaryotic organisms,and is associated with diverse biological activities such as hematopoiesis and the endoplasmic reticulum stress response.The disruption of UFMylation results in embryonic lethality in mice and is associated with various human diseases,thus underscoring its essential role in embryonic development,tissue morphogenesis,and organismal homeostasis.In this review,we aim to provide an in-depth overview of the UFMylation system,its importance in disease processes,and its potential as a novel target for therapeutic intervention.
关 键 词:UFMylation UFM1 post-translational modification DISEASE therapeutic target
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