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

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131 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 languageEnglish (US)
Pages (from-to)464-467
Number of pages4
JournalScience
Volume314
Issue number5798
DOIs
Publication statusPublished - Oct 20 2006
Externally publishedYes

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Cite this

Goley, E. D., Ohkawa, T., Mancuso, J., Woodruff, J. B., D'Alessio, J. A., Canda, W. Z., ... Welch, M. D. (2006). Dynamic nuclear actin assembly by Arp2/3 complex and a baculovirus WASP-like protein. Science, 314(5798), 464-467. https://doi.org/10.1126/science.1133348