Protein and non-protein targets of ubiquitin modification
Protein and non-protein targets of ubiquitin modification
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泛素修饰的蛋白质和非蛋白质靶标
DOI：
10.1152/ajpcell.00069.2023
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发表时间：
2023
影响因子：
5.5
通讯作者：
Ikeda Fumiyo
中科院分区：
文献类型：
--
作者：
Utama IV;Yamahira K;小林大純・山川宇宙・佐藤真央・前田 健・山平寿智;柿岡諒・Masengi KWA・木村亮介・山平寿智;Ikeda Fumiyo
泛素通过修饰不同的底物，通过许多不同的偶联类型调节多种生物功能。通常，泛素的c端通过异肽或肽键结合到蛋白质底物上。最近的研究表明，泛素可以形成一个非典型的氧酯键，它可以靶向蛋白质甚至非蛋白质底物，包括糖和脂质。非蛋白泛素化如何影响底物和细胞功能尚不完全清楚。本文综述了泛素化的最新发现及其对生物学的潜在影响。
Ubiquitin regulates a wide variety of biological functions by modifying diverse substrates, via many different conjugation types. Classically, the C-terminus of ubiquitin conjugates to protein substrates via an isopeptide or peptide bond. Recent studies revealed that ubiquitin can form an atypical oxyester bond, which can target protein and even nonproteinaceous substrates, including sugars and lipids. How nonprotein ubiquitination affects substrate and cellular functions is incompletely understood. This review covers recent discoveries in ubiquitination and its potential impacts on biology.