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SCFFBXO28-mediated self-ubiquitination of FBXO28 promotes its degradation

机译：SCFFBXO28介导的FBXO28的自我泛素促进其降解

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摘要

The F-box protein is the substrate recognition subunit of SCF (SKP1/CUL1/F-box) E3 ubiquitin ligase complex, a multicomponent RING-type E3 ligase involved in the regulation of numerous cellular processes by targeting critical regulatory proteins for ubiquitination. However, whether and how F-box proteins are regulated is largely unknown. Here we report that FBXO28, a poorly characterized F-box protein, is a novel substrate of SCF E3 ligase. Pharmaceutical or genetic inhibition of neddylation pathway that is required for the activation of SCF stabilizes FBXO28 and prolongs its half-life. Meanwhile, FBXO28 is subjected to ubiquitination and cullin1-based SCF complex promotes FBXO28 degradation. Moreover, deletion of F-box domain stabilizes FBXO28 and knockdown of endogenous FBXO28 strongly upregulates exogenous FBXO28 expression. Taken together, these data reveal that SCFFBXO28 is the E3 ligase responsible for the self-ubiquitination and proteasomal degradation of FBXO28, providing a new clue for the upstream signaling regulation for F-box proteins.
机译：F箱蛋白是SCF（SKP1 / CUL1 / F箱）E3泛素连接酶复合物的底物识别亚基，通过针对普遍突出的临界调节蛋白来调节许多细胞过程的多组分环型E3连接酶。然而，无论是如何调节F箱蛋白质的规定都是未知的。在这里，我们报告说FBXO28，一种表征不良的F箱蛋白，是SCF E3连接酶的新衬底。 SCF激活所需的萘酰化途径的药物或遗传抑制稳定FBXO28并延长其半衰期。同时，FBXO28经受泛素化，基于Cullin1的SCF复合物促进FBXO28降解。此外，缺失F箱结构域稳定FBXO28，内源FBXO28的敲低强烈上调外源FBXO28表达。总之，这些数据显示，SCFFBXO28是FBXO28的自矿量和蛋白酶体降解的E3连接酶，为F箱蛋白的上游信号传导调节提供了新的线索。

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