Dynamic nuclear actin assembly by Arp2/3 complex and a baculovirus WASP-like protein

Erin D. Goley; Taro Ohkawa; Joel Mancuso; Jeffrey B. Woodruff; Joseph A. D'Alessio; W. Zacheus Canda; Loy E. Volkman; Matthew D. Welch

doi:10.1126/science.1133348

Dynamic nuclear actin assembly by Arp2/3 complex and a baculovirus WASP-like protein

Erin D. Goley, Taro Ohkawa, Joel Mancuso, Jeffrey B. Woodruff, Joseph A. D'Alessio, W. Zacheus Canda, Loy E. Volkman, Matthew D. Welch

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

137 Scopus citations

Abstract

Diverse bacterial and viral pathogens induce actin polymerization in the cytoplasm of host cells to facilitate infection. Here, we describe a pathogenic mechanism for promoting dynamic actin assembly in the nucleus to enable viral replication. The baculovirus Autographa californica multiple nucleopolyhedrovirus induced nuclear actin polymerization by translocating the host actin-nucleating Arp2/3 complex into the nucleus, where it was activated by p78/83, a viral Wiskott-Aldrich syndrome protein (WASP)-like protein. Nuclear actin assembly by p78/83 and Arp2/3 complex was essential for viral progeny production. Recompartmentalizing dynamic host actin may represent a conserved mode of pathogenesis and reflect viral manipulation of normal functions of nuclear actin.

Original language	English (US)
Pages (from-to)	464-467
Number of pages	4
Journal	Science
Volume	314
Issue number	5798
DOIs	https://doi.org/10.1126/science.1133348
State	Published - Oct 20 2006
Externally published	Yes

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title = "Dynamic nuclear actin assembly by Arp2/3 complex and a baculovirus WASP-like protein",

abstract = "Diverse bacterial and viral pathogens induce actin polymerization in the cytoplasm of host cells to facilitate infection. Here, we describe a pathogenic mechanism for promoting dynamic actin assembly in the nucleus to enable viral replication. The baculovirus Autographa californica multiple nucleopolyhedrovirus induced nuclear actin polymerization by translocating the host actin-nucleating Arp2/3 complex into the nucleus, where it was activated by p78/83, a viral Wiskott-Aldrich syndrome protein (WASP)-like protein. Nuclear actin assembly by p78/83 and Arp2/3 complex was essential for viral progeny production. Recompartmentalizing dynamic host actin may represent a conserved mode of pathogenesis and reflect viral manipulation of normal functions of nuclear actin.",

author = "Goley, {Erin D.} and Taro Ohkawa and Joel Mancuso and Woodruff, {Jeffrey B.} and D'Alessio, {Joseph A.} and Canda, {W. Zacheus} and Volkman, {Loy E.} and Welch, {Matthew D.}",

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T1 - Dynamic nuclear actin assembly by Arp2/3 complex and a baculovirus WASP-like protein

AU - Goley, Erin D.

AU - Ohkawa, Taro

AU - Mancuso, Joel

AU - Woodruff, Jeffrey B.

AU - D'Alessio, Joseph A.

AU - Canda, W. Zacheus

AU - Volkman, Loy E.

AU - Welch, Matthew D.

PY - 2006/10/20

Y1 - 2006/10/20

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AB - Diverse bacterial and viral pathogens induce actin polymerization in the cytoplasm of host cells to facilitate infection. Here, we describe a pathogenic mechanism for promoting dynamic actin assembly in the nucleus to enable viral replication. The baculovirus Autographa californica multiple nucleopolyhedrovirus induced nuclear actin polymerization by translocating the host actin-nucleating Arp2/3 complex into the nucleus, where it was activated by p78/83, a viral Wiskott-Aldrich syndrome protein (WASP)-like protein. Nuclear actin assembly by p78/83 and Arp2/3 complex was essential for viral progeny production. Recompartmentalizing dynamic host actin may represent a conserved mode of pathogenesis and reflect viral manipulation of normal functions of nuclear actin.

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Dynamic nuclear actin assembly by Arp2/3 complex and a baculovirus WASP-like protein

Abstract

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