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首页> 外文期刊>Genes to cells : >Multiple roles of Rbx1 in the VBC-Cul2 ubiquitin ligase complex.
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Multiple roles of Rbx1 in the VBC-Cul2 ubiquitin ligase complex.

机译：Rbx1在VBC-Cul2泛素连接酶复合物中的多种作用。

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摘要

The importance of the ubiquitin system largely depends on ubiquitin ligases, E3s, as they determine the specificity of the system. Rbx1/ROC1/Hrt1, a RING finger protein, functions as an important component of the cullin-containing SCF and VBC-Cul2 ligases. Modification of cullins by NEDD8 (NEDDylation), has been shown to be essential for the E3 activity of both SCF and VBC-Cul2, and it was suggested that Rbx1 acts as the E3 for cullin NEDDylation. RING finger is composed of eight cysteine and histidine residues that bind to zinc ions. Rbx1 is a highly evolutionarily conserved protein; however, the eighth coordination residue in its RING finger is aspartate (D97) rather than cysteine. Substitution of D97 with each of the other 19 amino acids demonstrates that aspartate is superior to cysteine in cullin NEDDylation. Interestingly, however, different D97 mutants demonstrate different activities towards 6 cullins tested. Importantly, we were able to discriminate between the NEDDylating activity of Rbx1 andits involvement in the ubiquitylation reaction within the context of VBC-Cul2. Moreover, while Rbx1 is not involved in governing the stability of SCF, Rbx1 mutants destabilize VBC-Cul2. Taken together, these results indicate that various mechanisms regulate both the activities and the stability of cullin-based ligases.
机译：泛素系统的重要性在很大程度上取决于泛素连接酶E3，因为它们决定了系统的特异性。 Rbx1 / ROC1 / Hrt1是一种无名指蛋白，是含有cullin的SCF和VBC-Cul2连接酶的重要组成部分。已经证明通过NEDD8（NEDDylation）修饰cullins对于SCF和VBC-Cul2的E3活性都是必不可少的，并且建议Rbx1充当cullin NEDDylation的E3。无名指由八个与锌离子结合的半胱氨酸和组氨酸残基组成。 Rbx1是高度进化保守的蛋白;但是，其无名指上的第八个配体残基是天冬氨酸（D97）而不是半胱氨酸。 D97被其他19个氨基酸中的每一个取代，表明在谷氨酰胺NEDDylation中天冬氨酸优于半胱氨酸。然而，有趣的是，不同的D97突变体对6种被测cullins具有不同的活性。重要的是，我们能够区分Rbx1的NEDDylating活性和它在VBC-Cul2内参与泛素化反应的过程。此外，虽然Rbx1不参与控制SCF的稳定性，但Rbx1突变体使VBC-Cul2不稳定。两者合计，这些结果表明各种机制调节基于cullin的连接酶的活性和稳定性。

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