VprBP (DCAF1): a promiscuous substrate recognition subunit that incorporates into both RING-family CRL4 and HECT-family EDD/UBR5 E3 ubiquitin ligases.
VprBP (DCAF1): a promiscuous substrate recognition subunit that incorporates into both RING-family CRL4 and HECT-family EDD/UBR5 E3 ubiquitin ligases.
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VPRBP（DCAF1）：杂交的底物识别亚基，该亚基均包含在环室CRL4和Hect-family eDD/UBR5 E3 E3泛素连接酶中。
DOI：
10.1186/1471-2199-14-22
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发表时间：
2013-09-13
影响因子：
--
通讯作者：
Swanson PC
中科院分区：
文献类型：
--
作者：
Nakagawa T;Mondal K;Swanson PC
泛素修饰系统中的末端步骤依赖于E3泛素连接酶以促进泛素转移至蛋白质底物。E3连接酶的底物识别和泛素转移活性可以由单个多肽介导，或者可以依赖于单独的亚基。后一种组织在E3连接酶的最大类别RING家族的成员中特别普遍，尽管在E3连接酶的较小HECT家族的成员中也报道了这种类型的排列的实例。本文综述了最近的发现，揭示了令人惊讶的和独特的能力VprBP（DCAF 1）作为一个主要类别的E3连接酶，环型CRL 4连接酶和HECT型EDD/UBR 5连接酶的成员的底物识别亚基。通常由VprBP相关的E3连接酶调节的细胞过程，以及它们的靶向和病毒辅助蛋白的颠覆也进行了讨论。总而言之，这些研究提供了重要的见解，并提出了有关在CRL 4和EDD/UBR 5 E3连接酶的背景下调节或破坏VprBP功能的机制的有趣的新问题。
The terminal step in the ubiquitin modification system relies on an E3 ubiquitin ligase to facilitate transfer of ubiquitin to a protein substrate. The substrate recognition and ubiquitin transfer activities of the E3 ligase may be mediated by a single polypeptide or may rely on separate subunits. The latter organization is particularly prevalent among members of largest class of E3 ligases, the RING family, although examples of this type of arrangement have also been reported among members of the smaller HECT family of E3 ligases. This review describes recent discoveries that reveal the surprising and distinctive ability of VprBP (DCAF1) to serve as a substrate recognition subunit for a member of both major classes of E3 ligase, the RING-type CRL4 ligase and the HECT-type EDD/UBR5 ligase. The cellular processes normally regulated by VprBP-associated E3 ligases, and their targeting and subversion by viral accessory proteins are also discussed. Taken together, these studies provide important insights and raise interesting new questions regarding the mechanisms that regulate or subvert VprBP function in the context of both the CRL4 and EDD/UBR5 E3 ligases.
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