A new NEDD8-ligating system for cullin-4A
A new NEDD8-ligating system for cullin-4A
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DOI：
10.1101/gad.12.15.2263
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发表时间：
1998-08-01
影响因子：
10.5
通讯作者：
Kato, S
中科院分区：
文献类型：
--
作者：
Osaka, F;Kawasaki, H;Kato, S
NEDD8是一种泛素(Ub)样蛋白。在这里，我们报告了一种新的泛素化相关途径，用于NEDD8的修饰。NEDD8被类EL(Ub激活酶)激活，该复合体由APP-BP1和hUba3组成，分别与EL的氨基和羧基末端有很高的同源性，然后连接到hUbc12(酵母Ub结合酶Ubc12p的人类同源物)。NEDD8修饰的主要靶蛋白是Hs-cullin-4A(CuL-4A)，它是人类cullin/CDC53蛋白家族的成员，是多功能Ub-蛋白连接酶E3复合体的重要组成部分，在Ub介导的蛋白降解中起关键作用。
NEDD8 is a ubiquitin (Ub)-like protein. Here we report a novel ubiquitinylation-related pathway for modification by NEDD8. NEDD8 was activated by an El (Ub-activating enzyme)-like complex, consisting of APP-BP1 and hUba3 with high respective homologies to the amino-and carboxy-terminal regions of El and then linked to hUbc12 (a human homolog of yeast Ub-conjugating enzyme Ubc12p). The major target protein modified by NEDD8 was found to be Hs-cullin-4A (Cul-4A), a member of the family of human cullin/Cdc53 proteins functioning as an essential component of a multifunctional Ub-protein ligase E3 complex that has a critical role in Ub-mediated proteolysis.