The Lysine48-Based Polyubiquitin Chain Proteasomal Signal: Not a Single Child Anymore
The Lysine48-Based Polyubiquitin Chain Proteasomal Signal: Not a Single Child Anymore
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DOI：
10.1002/anie.201205656
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发表时间：
2013-01-01
影响因子：
16.6
通讯作者：
Ciechanover, Aaron
中科院分区：
文献类型：
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作者：
Kravtsova-Ivantsiv, Yelena;Sommer, Thomas;Ciechanover, Aaron
泛素(Ub)与蛋白质的结合参与了许多过程的调节。修饰作为反式的识别元件，其中下游效应器与修饰的蛋白质结合，并决定其命运和/或功能。多聚Ub链通过Ub的内部赖氨酸(Lys)-48连接，并锚定在底物的内部Lys残基上，已成为公认的蛋白酶体靶向和降解的典型信号。然而，最近的研究表明，信号更加多样化，基于其他内部连接的链，以及由Ub和Ub样蛋白组成的线性或异源链，甚至是单一Ub，都被蛋白酶体识别。此外，还描述了与内部赖氨酸以外的残基相连的链，所有这些链都挑战了当前的范式。
The conjugation of ubiquitin (Ub) to proteins is involved in the regulation of many processes. The modification serves as a recognition element in trans, in which downstream effectors bind to the modified protein and determine its fate and/or function. A polyUb chain that is linked through internal lysine(Lys)-48 of Ub and anchored to an internal Lys residue of the substrate has become the accepted "canonical" signal for proteasomal targeting and degradation. However, recent studies show that the signal is far more diverse and that chains based on other internal linkages, as well as linear or heterologous chains made of Ub and Ub-like proteins and even monoUb, are recognized by the proteasome. In addition, chains linked to residues other than internal Lys were described, all challenging the current paradigm.