HIV-1 Nef interacts with the cyclin K/CDK13 complex to antagonize SERINC5 for optimal viral infectivity

文献类型： 外文期刊

第一作者： Li, Sunan

作者： Li, Sunan;Li, Rongrong;Ahmad, Iqbal;Zheng, Yong-Hui;Chai, Qingqing;Collins, Morgan K.;Johnson, Silas F.;Frabutt, Dylan A.;Zheng, Yong-Hui;Yang, Zhichang;Shen, Xiaojing;Sun, Liangliang;Hu, Jian;Hu, Jian;Johnson, Silas F.;Hultquist, Judd F.;Peterlin, B. Matija;Peterlin, B. Matija

作者机构：

期刊名称：CELL REPORTS （ 影响因子：9.423； 五年影响因子：10.394 ）

ISSN： 2211-1247

年卷期： 2021 年 36 卷 6 期

页码：

收录情况： SCI

摘要： HIV-1-negative factor (Nef) protein antagonizes serine incorporator 5 (SERINC5) by redirecting this potent restriction factor to the endosomes and lysosomes for degradation. However, the precise mechanism remains unclear. Using affinity purification/mass spectrometry, we identify cyclin K (CycK) and cyclin-dependent kinase 13 (CDK13) as a Nef- associated kinase complex. CycK/CDK13 phosphorylates the serine at position 360 (S360) in SERINC5, which is required for Nef downregulation of SERINC5 from the cell surface and its counteractivity of the SERINC5 antiviral activity. To understand the role of S360 phosphorylation, we generate chimeric proteins between CD8 and SERINC5 to study their response to Nef. Nef not only downregulates but, importantly, also binds to this chimera in an S360-dependent manner. Thus, S360 phosphorylation increases interactions between Nef and SERINC5 and initiates the destruction of SERINC5 by the endocytic machinery.

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