HIV-1 诱导的 CPSF6 向生物分子凝聚体的转运。

IF 14 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY Trends in Microbiology Pub Date : 2024-08-01 Epub Date: 2024-01-23 DOI:10.1016/j.tim.2024.01.001
Katarzyna Bialas, Felipe Diaz-Griffero
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引用次数: 0

摘要

裂解和多腺苷酸化特异性因子亚基 6(CPSF6,又称 CFIm68)是哺乳动物裂解因子 I(CFIm)复合物的一个 68 kDa 组份,可调节 mRNA 替代多腺苷酸化(APA)并决定 3' 非翻译区(UTR)长度,这是一种重要的基因表达控制机制。CPSF6 在感染过程中与 HIV-1 核心直接相互作用,表明它参与了 HIV-1 的复制。在此,我们回顾了 CPSF6 对 HIV-1 复制周期各个阶段的贡献。最近,几个研究小组描述了 HIV-1 感染诱导 CPSF6 转位至核斑点(一种生物分子凝聚物)的能力。我们讨论了 CPSF6 在凝聚体中定位的意义,以及凝聚体定位的 CPSF6 在 HIV-1 控制细胞蛋白质表达模式的能力中的潜在作用。
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HIV-1-induced translocation of CPSF6 to biomolecular condensates.

Cleavage and polyadenylation specificity factor subunit 6 (CPSF6, also known as CFIm68) is a 68 kDa component of the mammalian cleavage factor I (CFIm) complex that modulates mRNA alternative polyadenylation (APA) and determines 3' untranslated region (UTR) length, an important gene expression control mechanism. CPSF6 directly interacts with the HIV-1 core during infection, suggesting involvement in HIV-1 replication. Here, we review the contributions of CPSF6 to every stage of the HIV-1 replication cycle. Recently, several groups described the ability of HIV-1 infection to induce CPSF6 translocation to nuclear speckles, which are biomolecular condensates. We discuss the implications for CPSF6 localization in condensates and the potential role of condensate-localized CPSF6 in the ability of HIV-1 to control the protein expression pattern of the cell.

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来源期刊
Trends in Microbiology
Trends in Microbiology 生物-生化与分子生物学
CiteScore
25.30
自引率
0.60%
发文量
193
审稿时长
6-12 weeks
期刊介绍: Trends in Microbiology serves as a comprehensive, multidisciplinary forum for discussing various aspects of microbiology, spanning cell biology, immunology, genetics, evolution, virology, bacteriology, protozoology, and mycology. In the rapidly evolving field of microbiology, technological advancements, especially in genome sequencing, impact prokaryote biology from pathogens to extremophiles, influencing developments in drugs, vaccines, and industrial enzyme research.
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