F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
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DOI：
10.1016/s0092-8674(00)80403-1
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发表时间：
1997-10-17
期刊：
影响因子：
64.5
通讯作者：
Harper, JW
中科院分区：
文献类型：
--
作者：
Skowyra, D;Craig, KL;Harper, JW
我们使用重组蛋白重建了Cdk抑制剂Sic 1的泛素化途径。Skp 1、Cdc 53和F-box蛋白Cdc 4形成复合物SCFCdc 4，其作为Sic 1泛素连接酶（E3）与泛素缀合酶（E2）Cdc 34和E1组合起作用。Cdc 4与Skp 1组装，作为选择性结合磷酸化Sic 1的受体发挥功能。Grr 1是一种参与Cln破坏的F盒蛋白，与Skp 1和Cdc 53形成复合物，并结合磷酸化的Cln 1和Cln 2，但不结合Sic 1。由于SCF复合物的成分是蛋白质家族的成员，因此SCFCdc 4可能作为由相关家族成员的组合相互作用形成的一大类E3的原型。SCF复合物将蛋白激酶信号传导途径与蛋白质丰度的控制偶联。
We have reconstituted the ubiquitination pathway for the Cdk inhibitor Sic1 using recombinant proteins. Skp1, Cdc53, and the F-box protein Cdc4 form a complex, SCFCdc4, which functions as a Sic1 ubiquitin-ligase (E3) in combination with the ubiquitin conjugating enzyme (E2) Cdc34 and E1. Cdc4 assembled with Skp1 functions as the receptor that selectively binds phosphorylated Sic1. Grr1, an F-box protein involved in Cln destruction, forms complexes with Skp1 and Cdc53 and binds phosphorylated Cln1 and Cln2, but not Sic1. Because the constituents of the SCF complex are members of protein families, SCFCdc4 in likely to serve as the prototype for a large class of E3s formed by combinatorial interactions of related family members. SCF complexes couple protein kinase signaling pathways to the control of protein abundance.