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

Jingfang Mu; Yongli Zhang; Yangyang Hu; Xue Hu; Yuan Zhou; He Zhao; Rongjuan Pei; Chunchen Wu; Jizheng Chen; Han Zhao; Kai Yang; Monique van Oers; Xinwen Chen; Yun Wang

doi:10.1371/journal.ppat.1005994

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

Jingfang Mu, Yongli Zhang, Yangyang Hu, Xue Hu, Yuan Zhou, He Zhao, Rongjuan Pei, Chunchen Wu, Jizheng Chen, Han Zhao, Kai Yang, Monique van Oers, Xinwen Chen^*, Yun Wang

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

19 Citations (Scopus)

Abstract

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.

Original language	English
Article number	e1005994
Journal	PLoS Pathogens
Volume	12
Issue number	11
DOIs	https://doi.org/10.1371/journal.ppat.1005994
Publication status	Published - 2016

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Mu, J., Zhang, Y., Hu, Y., Hu, X., Zhou, Y., Zhao, H., Pei, R., Wu, C., Chen, J., Zhao, H., Yang, K., van Oers, M., Chen, X., & Wang, Y. (2016). Autographa californica Multiple Nucleopolyhedrovirus Ac34 Protein Retains Cellular Actin-Related Protein 2/3 Complex in the Nucleus by Subversion of CRM1-Dependent Nuclear Export. PLoS Pathogens, 12(11), Article e1005994. https://doi.org/10.1371/journal.ppat.1005994

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

abstract = "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.",

author = "Jingfang Mu and Yongli Zhang and Yangyang Hu and Xue Hu and Yuan Zhou and He Zhao and Rongjuan Pei and Chunchen Wu and Jizheng Chen and Han Zhao and Kai Yang and {van Oers}, Monique and Xinwen Chen and Yun Wang",

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language = "English",

volume = "12",

journal = "PLoS Pathogens",

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Mu, J, Zhang, Y, Hu, Y, Hu, X, Zhou, Y, Zhao, H, Pei, R, Wu, C, Chen, J, Zhao, H, Yang, K, van Oers, M, Chen, X & Wang, Y 2016, 'Autographa californica Multiple Nucleopolyhedrovirus Ac34 Protein Retains Cellular Actin-Related Protein 2/3 Complex in the Nucleus by Subversion of CRM1-Dependent Nuclear Export', PLoS Pathogens, vol. 12, no. 11, e1005994. https://doi.org/10.1371/journal.ppat.1005994

TY - JOUR

T1 - Autographa californica Multiple Nucleopolyhedrovirus Ac34 Protein Retains Cellular Actin-Related Protein 2/3 Complex in the Nucleus by Subversion of CRM1-Dependent Nuclear Export

AU - Mu, Jingfang

AU - Zhang, Yongli

AU - Hu, Yangyang

AU - Hu, Xue

AU - Zhou, Yuan

AU - Zhao, He

AU - Pei, Rongjuan

AU - Wu, Chunchen

AU - Chen, Jizheng

AU - Zhao, Han

AU - Yang, Kai

AU - van Oers, Monique

AU - Chen, Xinwen

AU - Wang, Yun

PY - 2016

Y1 - 2016

N2 - 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.

AB - 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.

U2 - 10.1371/journal.ppat.1005994

DO - 10.1371/journal.ppat.1005994

M3 - Article

AN - SCOPUS:85002328291

SN - 1553-7366

VL - 12

JO - PLoS Pathogens

JF - PLoS Pathogens

IS - 11

M1 - e1005994

ER -

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

Abstract

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