NEDD8与泛素E2缀合酶之间的直接相互作用上调了基于cullin的E3连接酶活性。
Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity.
作者信息
Sakata Eri, Yamaguchi Yoshiki, Miyauchi Yasuhiro, Iwai Kazuhiro, Chiba Tomoki, Saeki Yasushi, Matsuda Noriyuki, Tanaka Keiji, Kato Koichi
机构信息
Department of Structural Biology and Biomolecular Engineering, Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan.
出版信息
Nat Struct Mol Biol. 2007 Feb;14(2):167-8. doi: 10.1038/nsmb1191. Epub 2007 Jan 7.
Although cullin-1 neddylation is crucial for the activation of SCF ubiquitin E3 ligases, the underlying mechanisms for NEDD8-mediated activation of SCF remain unclear. Here we demonstrate by NMR and mutational studies that NEDD8 binds the ubiquitin E2 (UBC4), but not NEDD8 E2 (UBC12). Our data imply that NEDD8 forms an active platform on the SCF complex for selective recruitment of ubiquitin-charged E2s in collaboration with RBX1, and thereby upregulates the E3 activity.
尽管cullin-1的NEDD8化对于SCF泛素E3连接酶的激活至关重要，但NEDD8介导的SCF激活的潜在机制仍不清楚。在这里，我们通过核磁共振和突变研究证明，NEDD8结合泛素E2（UBC4），但不结合NEDD8 E2（UBC12）。我们的数据表明，NEDD8在SCF复合物上形成一个活性平台，与RBX1协同作用，选择性招募带泛素的E2，从而上调E3活性。
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