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首页> 外文期刊>Journal of Molecular Biology >MUF1/leucine-rich repeat containing 41 (LRRC41), a substrate of RhoBTB-dependent cullin 3 ubiquitin ligase complexes, is a predominantly nuclear dimeric protein
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MUF1/leucine-rich repeat containing 41 (LRRC41), a substrate of RhoBTB-dependent cullin 3 ubiquitin ligase complexes, is a predominantly nuclear dimeric protein

机译：富含MUF1 /亮氨酸的重复序列，包含41（LRRC41），是依赖RhoBTB的cullin 3泛素连接酶复合物的底物，主要是核二聚体蛋白

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RhoBTB (BTB stands for broad-complex, tramtrack, bric à brac) proteins are tumor suppressors involved in the formation of cullin 3 (Cul3)-dependent ubiquitin ligase complexes. However, no substrates of RhoBTB-Cul3 ubiquitin ligase complexes have been identified. We identified MUF1 (LRRC41, leucine-rich repeat containing 41) as a potential interaction partner of RhoBTB3 in a two-hybrid screening on a mouse brain cDNA library. MUF1 is a largely uncharacterized protein containing a leucine-rich repeat and, interestingly, a BC-box that serves as a linker in multicomponent, cullin 5 (Cul5)-based ubiquitin ligases. We confirmed the interaction of MUF1 with all three mammalian RhoBTB proteins using immunoprecipitation. We characterized MUF1 in terms of expression profile and subcellular localization, the latter also with respect to RhoBTB proteins. We found out that MUF1 is a ubiquitously expressed nuclear protein that, upon coexpression with RhoBTB, partially retains in the cytoplasm, where both proteins colocalize. We also show that MUF1 is able to dimerize similarly to other leucine-rich repeat-containing proteins. To explore the significance of MUF1-RhoBTB interaction within Cul-ligase complexes and the mechanism of MUF1 degradation, we performed a protein stability assay and found that MUF1 is degraded in the proteasome in a Cul5-independent manner by RhoBTB3-Cul3 ubiquitin ligase complex. Finally, we explored a possible heterodimerization of Cul3 and Cul5 and indeed discovered that these two cullins are capable of forming heterodimers. Thus, we have identified MUF1 as the first substrate for RhoBTB-Cul3 ubiquitin ligase complexes. Identification of substrates of these complexes will result in better understanding of the tumor suppressor function of RhoBTB.
机译：RhoBTB（BTB代表宽复合体，电车轨道，bricàbrac）蛋白是肿瘤抑制因子，参与形成依赖于cullin 3（Cul3）的泛素连接酶复合物。但是，尚未发现RhoBTB-Cul3泛素连接酶复合物的底物。我们在鼠标大脑cDNA文库的两次杂交筛选中确定MUF1（LRRC41，富含41的亮氨酸重复序列）是RhoBTB3的潜在相互作用伴侣。 MUF1是一个很大程度上未鉴定的蛋白质，含有富含亮氨酸的重复序列，有趣的是，BC-box在多组分，基于cullin 5（Cul5）的泛素连接酶中充当接头。我们使用免疫沉淀证实了MUF1与所有三个哺乳动物RhoBTB蛋白的相互作用。我们根据表达谱和亚细胞定位来表征MUF1，后者也针对RhoBTB蛋白。我们发现，MUF1是一种普遍表达的核蛋白，与RhoBTB共表达后，部分保留在细胞质中，这两种蛋白都共定位。我们还表明，MUF1能够与其他富含亮氨酸的重复序列重复蛋白相似地二聚。为了探索Cul-连接酶复合物中MUF1-RhoBTB相互作用的重要性和MUF1降解的机理，我们进行了蛋白质稳定性分析，发现RhoBTB3-Cul3泛素连接酶复合物以Cul5独立的方式降解了MUF1在蛋白酶体中的降解。最后，我们探索了Cul3和Cul5的可能异源二聚体，并确实发现这两种cullins能够形成异源二聚体。因此，我们已经确定MUF1为RhoBTB-Cul3泛素连接酶复合物的第一个底物。这些复合物的底物的识别将导致更好地了解RhoBTB的肿瘤抑制功能。

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