Department of Biological and Environmental Sciences, Le Moyne College, Syracuse, NY 13214, USA.
Viruses. 2024 Aug 17;16(8):1313. doi: 10.3390/v16081313.
The Human Immunodeficiency Virus (HIV) encodes several proteins that contort the host cell environment to promote viral replication and spread. This is often accomplished through the hijacking of cellular ubiquitin ligases. These reprogrammed complexes initiate or enhance the ubiquitination of cellular proteins that may otherwise act to restrain viral replication. Ubiquitination of target proteins may alter protein function or initiate proteasome-dependent destruction. HIV Viral Protein R (Vpr) and the related HIV-2 Viral Protein X (Vpx), engage the CRL4-DCAF1 ubiquitin ligase complex to target numerous cellular proteins. In this review we describe the CRL4-DCAF1 ubiquitin ligase complex and its interactions with HIV Vpr and Vpx. We additionally summarize the cellular proteins targeted by this association as well as the observed or hypothesized impact on HIV.
人类免疫缺陷病毒 (HIV) 编码几种蛋白,这些蛋白扭曲宿主细胞环境以促进病毒复制和传播。这通常是通过劫持细胞泛素连接酶来实现的。这些重编程的复合物启动或增强细胞蛋白的泛素化,这些蛋白原本可能会抑制病毒复制。靶蛋白的泛素化可能会改变蛋白功能或启动蛋白酶体依赖性降解。HIV 病毒蛋白 R (Vpr) 和相关的 HIV-2 病毒蛋白 X (Vpx),与 CRL4-DCAF1 泛素连接酶复合物结合,以靶向许多细胞蛋白。在这篇综述中,我们描述了 CRL4-DCAF1 泛素连接酶复合物及其与 HIV Vpr 和 Vpx 的相互作用。我们还总结了该复合物靶向的细胞蛋白,以及观察到或假设的对 HIV 的影响。