Involvement of the βTrCP in the ubiquitination and stability of the HIV-1 Vpu protein
Involvement of the βTrCP in the ubiquitination and stability of the HIV-1 Vpu protein
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DOI：
10.1016/j.bbrc.2007.03.195
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发表时间：
2007-06-08
影响因子：
3.1
通讯作者：
Besnard-Guerin, Corinne
中科院分区：
文献类型：
--
作者：
Belaidouni, Nadia;Marchal, Christelle;Besnard-Guerin, Corinne
人类免疫缺陷病毒 I 型 (HIV-1) Vpu 蛋白与 CD4 受体结合，并将其靶向蛋白酶体进行降解。该过程需要招募人 β TrCP，它是 Skp1-Cullin-F 盒 (SCF) 泛素连接酶复合物的一个组成部分，可与磷酸化的 Vpu 分子相互作用。与 PTrCP 的其他配体不同，Vpu 从未被报道被降解。我们提供的证据表明 Vpu 本身被泛素化并被蛋白酶体降解。我们证明，不能与 PTrCP 相互作用的突变体 Vpu2.6 是稳定的，并且与野生型 Vpu 不同，它不是多泛素化的。这些结果表明 PTrCP 参与 Vpu 多泛素化。 (c) 2007 Elsevier Inc. 保留所有权利。
The human immunodeficiency virus type I (HIV-1) Vpu protein binds to the CD4 receptor and targets it to the proteasome for degradation. This process requires the recruitment of human beta TrCP, a component of the Skp1-Cullin-F box (SCF) ubiquitin ligase complex, that interacts with phosphorylated Vpu molecules. Vpu, unlike other ligands of PTrCP, has never been reported to be degraded. We provide evidence that Vpu, itself, is ubiquitinated and targeted for degradation by the proteasome. We demonstrate that the mutant Vpu2.6, which cannot interact with PTrCP, is stable and, unlike wild-type Vpu, is not polyubiquitinated. These results suggest that PTrCP is involved in Vpu polyubiquitination. (c) 2007 Elsevier Inc. All rights reserved.