Dynamic Nuclear Actin Assembly by Arp2/3 Complex and a Baculovirus WASP-Like Protein

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

doi:10.1126/science.1133348

Cited by 159 publications

(202 citation statements)

References 18 publications

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“…The polymerization of nuclear actin into dense, stable and phalloidin-stainable nuclear actin filaments occurs in some pathological conditions, such as skeletal myopathies (Domazetovska et al, 2007b), baculovirus infection (Goley et al, 2006) and idiopathic inflammatory myopathy (Stenzel et al, 2015). Nuclear actin filaments have also been noted following treatment with actin-depolymerizing drugs (Belin et al, 2013;Sen et al, 2015;Yahara et al, 1982) and upon dysregulation of actin-binding proteins such as exportin-6 (Dopie et al, 2015(Dopie et al, , 2012 and MICAL-2 (Lundquist et al, 2014).…”

Section: Introductionmentioning

confidence: 98%

Persistent nuclear actin filaments inhibit transcription by RNA polymerase II

Serebryannyy

Parilla

Annibale

et al. 2016

Journal of Cell Science

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Actin is abundant in the nucleus and it is clear that nuclear actin has important functions. However, mystery surrounds the absence of classical actin filaments in the nucleus. To address this question, we investigated how polymerizing nuclear actin into persistent nuclear actin filaments affected transcription by RNA polymerase II. Nuclear filaments impaired nuclear actin dynamics by polymerizing and sequestering nuclear actin. Polymerizing actin into stable nuclear filaments disrupted the interaction of actin with RNA polymerase II and correlated with impaired RNA polymerase II localization, dynamics, gene recruitment, and reduced global transcription and cell proliferation. Polymerizing and crosslinking nuclear actin in vitro similarly disrupted the actin-RNA-polymerase-II interaction and inhibited transcription. These data rationalize the general absence of stable actin filaments in mammalian somatic nuclei. They also suggest a dynamic pool of nuclear actin is required for the proper localization and activity of RNA polymerase II.

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Section: Introductionmentioning

confidence: 98%

Persistent nuclear actin filaments inhibit transcription by RNA polymerase II

Serebryannyy

Parilla

Annibale

et al. 2016

Journal of Cell Science

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“…Similarly, academic research studying, e.g., the underpinnings of viral pathogenesis (Goley et al, 2006) utilize ultrapure viral dispersions with minimum DNA and host cell protein levels.…”

Section: Introductionmentioning

confidence: 99%

Purification of a recombinant baculovirus of Autographa californica M nucleopolyhedrovirus by ion exchange membrane chromatography

Grein

Michalsky

López

et al. 2012

Journal of Virological Methods

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“…Baculovirus-infected cells also form nuclear actin filaments at the time of virus assembly; these filaments co-localize with nucleocapsids and the baculovirus major capsid protein binds to F-actin [39]. The baculovirus protein p78/83 shares homology with WASP, a nucleator of actin, and promotes actin filament polymerization directly [40]. Herpesviruses do not seem to encode a homologous protein.…”

Section: Viral Replication and Capsid Assembly In The Nucleusmentioning

confidence: 99%

Actin and Rho GTPases in herpesvirus biology

Favoreel¹,

Enquist²,

Feierbach³

2007

Trends in Microbiology

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Viruses have evolved a variety of interactions with host cells to create an optimal niche for viral replication, persistence and spread. The actin cytoskeleton of the host cell and actin-regulating Rho GTPase signaling pathways can be involved in several of these interactions. This review focuses on recent findings on herpesvirus interactions with actin and Rho GTPases during viral entry, replication in the nucleus and egress. Unraveling these often fascinating interactions might also provide additional insights into sometimes poorly known aspects of actin biology (e.g. its role in the nucleus) and in the development of novel antiviral therapies.Actin filaments and actin-regulating Rho GTPase signaling pathways Filamentous actin is a key structure of the cytoskeleton in every cell. The actin cytoskeleton is involved in many crucial cellular processes, including providing cell integrity, mobility and shape; driving cell division and contraction; and the uptake of extracellular molecules.Actin filaments consist of polarized ATP-bound globular actin monomers. These filamentous actin (F-actin) molecules can associate into bundles or networks through actin cross-linking molecules. The best characterized F-actin bundles and networks are filopodia, lamellipodia and actin stress fibers. Formation of the different actin bundles and networks is regulated by signal transduction pathways that depend on small Rho GTPases [1]. Of the 22 identified mammalian Rho GTPases, the best characterized are RhoA (stress fibers), Rac1 (lamellipodia) and Cdc42 (filopodia). These Rho GTPases act as molecular switches and alternate between their active GTP-bound form and their inactive GDP-bound form. Transition from the active to the inactive form is accompanied by phosphorylation and activation of different downstream effector molecules that initiate signal transduction pathways and subsequent rearrangements in the actin cytoskeleton. These three signal transduction pathways are interwoven and the RhoA pathway generally counteracts the Rac1 and Cdc42 pathways [2]. Details of Rho GTPase signaling networks can be found elsewhere [3].Because of the many cellular functions in which they are involved, it comes as no surprise that many intracellular pathogens interact with actin and actin-regulating signaling pathways. These interactions can occur at several points in the life cycle of the pathogens, including, although not limited to, internalization, intracellular movement and intercellular spread [4,5].There are recent indications that, in particular cell types, herpesviruses also interact with actin and/or Rho GTPases during three major phases of the replication cycle of herpesviruses: entry into the cytoplasm, replication and assembly in the nucleus and maturation and egress. This review presents an overview of these data and points to future directions in research in this new and potentially important field of herpesvirus biology. Special attention is given on the alphaherpesvirus subfamily of herpesviruses, but relevant references to wor...

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Dynamic Nuclear Actin Assembly by Arp2/3 Complex and a Baculovirus WASP-Like Protein

Cited by 159 publications

References 18 publications

Persistent nuclear actin filaments inhibit transcription by RNA polymerase II

Persistent nuclear actin filaments inhibit transcription by RNA polymerase II

Purification of a recombinant baculovirus of Autographa californica M nucleopolyhedrovirus by ion exchange membrane chromatography

Actin and Rho GTPases in herpesvirus biology

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