Autographa californica Multiple Nucleopolyhedrovirus Ac34 Protein Retains Cellular Actin-Related Protein 2/3 Complex in the Nucleus by Subversion of CRM1-Dependent Nuclear Export.

Autographa californica Multiple Nucleopolyhedrovirus Ac34 Protein Retains Cellular Actin-Related Protein 2/3 Complex in the Nucleus by Subversion of CRM1-Dependent Nuclear Export.
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苜蓿银纹夜蛾多核多角体病毒 Ac34 蛋白通过破坏 CRM1 依赖性核输出将细胞肌动蛋白相关蛋白 2/3 复合物保留在细胞核中

DOI:
10.1371/journal.ppat.1005994
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发表时间:
2016-11
期刊:
影响因子:
6.7
通讯作者:
Wang Y
Wang Y
中科院分区:
医学1区
文献类型:
--
作者:
Mu J;Zhang Y;Hu Y;Hu X;Zhou Y;Zhao H;Pei R;Wu C;Chen J;Zhao H;Yang K;Oers MM;Chen X;Wang Y

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肌动蛋白、成核促进因子(NPFs)和肌动蛋白相关蛋白2/3复合物(Arp 2/3)是细胞肌动蛋白聚合机制的关键要素。随着核内肌动蛋白聚合在生物学过程中的广泛应用以及肌动蛋白和核转录因子核内转运机制的发现,确定Arp 2/3核质穿梭机制对于理解核内肌动蛋白的功能具有重要意义。昆虫细胞的甲杆状病毒感染的一个独特特征是Arp 2/3在细胞核中的大量积累,其诱导细胞核中的肌动蛋白聚合以帮助病毒复制。我们发现Ac 34是苜蓿银纹夜蛾核型多角体病毒(Autographa californica multiple nucleopolyhedrovirus,AcMNPV)编码的一种病毒晚期基因产物,在病毒感染过程中参与Arp 2/3的核积累。进一步的分析表明,Arp 2/3在稳态条件下的亚细胞分布是由染色体维持1(CRM 1)依赖的核输出控制的。AcMNPV感染后,Ac 34抑制CRM 1通路并导致Arp 2/3滞留在核中。
Actin, nucleation-promoting factors (NPFs), and the actin-related protein 2/3 complex (Arp2/3) are key elements of the cellular actin polymerization machinery. With nuclear actin polymerization implicated in ever-expanding biological processes and the discovery of the nuclear import mechanisms of actin and NPFs, determining Arp2/3 nucleo-cytoplasmic shuttling mechanism is important for understanding the function of nuclear actin. A unique feature of alphabaculovirus infection of insect cells is the robust nuclear accumulation of Arp2/3, which induces actin polymerization in the nucleus to assist in virus replication. We found that Ac34, a viral late gene product encoded by the alphabaculovirus Autographa californica multiple nucleopolyhedrovirus (AcMNPV), is involved in Arp2/3 nuclear accumulation during virus infection. Further assays revealed that the subcellular distribution of Arp2/3 under steady-state conditions is controlled by chromosomal maintenance 1 (CRM1)-dependent nuclear export. Upon AcMNPV infection, Ac34 inhibits CRM1 pathway and leads to Arp2/3 retention in the nucleus.
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