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
中科院分区:
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
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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DOI:
10.1038/nrm2867
发表时间:
2010-04
期刊:
Nature reviews. Molecular cell biology
影响因子:
--
作者:
通讯作者:
--
影响因子:
64.5
作者:
Fornerod, M;Ohno, M;Mattaj, IW
通讯作者:
Mattaj, IW
影响因子:
16.6
作者:
通讯作者:
--
影响因子:
5.4
作者:
Kopecky-Bromberg, Sarah A.;Martinez-Sobrido, Luis;Palese, Peter
通讯作者:
Palese, Peter
影响因子:
6.7
作者:
Feierbach B;Piccinotti S;Bisher M;Denk W;Enquist LW
通讯作者:
Enquist LW