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Modification of Cul1 regulates its association with proteasomal subunits

机译：Cul1的修饰调节其与蛋白酶体亚基的关联

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Background Ubiquitylation targets proteins for degradation by the 26S proteasome. Some yeast and plant ubiquitin ligases, including the highly conserved SCF ( S kp1/ C ul1/ F -box protein) complex, have been shown to associate with proteasomes. We sought to characterize interactions between SCF complexes and proteasomes in mammalian cells. Results We found that the binding of SCF complexes to proteasomes is conserved in higher eukaryotes. The Cul1 subunit associated with both sub-complexes of the proteasome, and high molecular weight forms of Cul1 bound to the 19S proteasome. Cul1 is ubiquitylated in vivo. Ubiquitylation of Cul1 promotes its binding to the S5a subunit of the 19S sub-complex without affecting Cul1 stability. Conclusion The association of ubiquitylating enzymes with proteasomes may be an additional means to target ubiquitylated substrates for degradation.
机译：背景泛素化作用将蛋白质靶向26S蛋白酶体降解。一些酵母和植物遍在蛋白连接酶，包括高度保守的SCF（S kp1 / Cul1 / F-box蛋白）复合物，已显示与蛋白酶体相关。我们试图表征哺乳动物细胞中SCF复合体和蛋白酶体之间的相互作用。结果我们发现，SCF复合物与蛋白酶体的结合在高等真核生物中是保守的。与蛋白酶体的两个亚复合体以及与19S蛋白酶体结合的高分子量形式的Cul1相关的Cul1亚基。 Cul1在体内被泛素化。 Cul1的泛素化促进其与19S亚复合体的S5a亚基的结合，而不会影响Cul1的稳定性。结论泛素化酶与蛋白酶体的结合可能是靶向泛素化底物降解的另一种方法。

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