CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex
CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex
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DOI：
10.1016/s1097-2765(02)00784-0
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发表时间：
2002-12-01
期刊：
影响因子：
16
通讯作者：
Zhang, H
中科院分区：
文献类型：
--
作者：
Zheng, JY;Yang, XM;Zhang, H
SCF泛素E3连接酶调节许多调节蛋白如p27（Kip 1）、IkappaB和β-连环蛋白的泛素依赖性蛋白水解。我们报告分离的CUL 1结合蛋白，p120（CAND 1）。我们发现CUL 1的大部分与CAND 1和ROC 1形成复合物，而不依赖于SKP 1和F盒蛋白SKP 2。在体内和体外，CAND 1阻止SKP 1和SKP 2与CUL 1的结合，而CAND 1从CUL 1的解离促进逆反应。CUL 1的Neddylation或SKP 1和ATP的存在导致CAND 1解离。我们的数据表明，CAND 1调节SCF复合物的形成，其从CUL 1的解离与F盒蛋白掺入SCF复合物，导致其不稳定。
The SCF ubiquitin E3 ligase regulates ubiquitin-dependent proteolysis of many regulatory proteins such as p27(Kip1), IkappaB, and beta-catenin. We report the isolation of a CUL1 binding protein, p120(CAND1). We found the majority of CUL1 is in a complex with CAND1 and ROC1 independent of SKP1 and F box protein SKP2. Both in vivo and in vitro, CAND1 prevents the binding of SKP1 and SKP2 to CUL1 while dissociation of CAND1 from CUL1 promotes the reverse reaction. Neddylation of CUL1 or the presence of SKP1 and ATP causes CAND1 dissociation. Our data suggest that CAND1 regulates the formation of the SCF complex, and its dissociation from CUL1 is coupled with the incorporation of F box proteins into the SCF complex, causing their destabilization.