Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3

Natalie Leach; Susan L Bjerke; Desire K Christensen; Jacques M Bouchard; Fan Mou; Richard Park; Joel Baines; Tokuko Haraguchi; Richard J Roller

doi:10.1128/JVI.00196-07

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Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3

Journal article

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Peer reviewed

Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3

Natalie Leach, Susan L Bjerke, Desire K Christensen, Jacques M Bouchard, Fan Mou, Richard Park, Joel Baines, Tokuko Haraguchi and Richard J Roller

Journal of virology, Vol.81(19), pp.10792-10803

10/2007

DOI: 10.1128/JVI.00196-07

PMCID: PMC2045475

PMID: 17652388

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Abstract

Cells infected with wild-type herpes simplex virus type 1 (HSV-1) show disruption of the organization of the nuclear lamina that underlies the nuclear envelope. This disruption is reflected in changes in the localization and phosphorylation of lamin proteins. Here, we show that HSV-1 infection causes relocalization of the LEM domain protein emerin. In cells infected with wild-type virus, emerin becomes more mobile in the nuclear membrane, and in cells infected with viruses that fail to express UL34 protein (pUL34) and US3 protein (pUS3), emerin no longer colocalizes with lamins, suggesting that infection causes a loss of connection between emerin and the lamina. Infection causes hyperphosphorylation of emerin in a manner dependent upon both pUL34 and pUS3. Some emerin hyperphosphorylation can be inhibited by the protein kinase Cdelta (PKCdelta) inhibitor rottlerin. Emerin and pUL34 interact physically, as shown by pull-down and coimmunoprecipitation assays. Emerin expression is not, however, necessary for infection, since virus growth is not impaired in cells derived from emerin-null transgenic mice. The results suggest a model in which pUS3 and PKCdelta that has been recruited by pUL34 hyperphosphorylate emerin, leading to disruption of its connections with lamin proteins and contributing to the disruption of the nuclear lamina. Changes in emerin localization, nuclear shape, and lamin organization characteristic of cells infected with wild-type HSV-1 also occur in cells infected with recombinant virus that does not make viral capsids, suggesting that these changes occur independently of capsid envelopment.

Amino Acid Sequence

Phosphorylation

Green Fluorescent Proteins - analysis

Nuclear Proteins - analysis

Herpesvirus 1, Human - metabolism

Humans

Protein-Serine-Threonine Kinases - genetics

Molecular Sequence Data

Viral Proteins - genetics

Nuclear Proteins - metabolism

Green Fluorescent Proteins - genetics

Viral Proteins - metabolism

Membrane Proteins - analysis

Nuclear Envelope - chemistry

Herpes Simplex - metabolism

Protein Kinase C-delta - metabolism

Nuclear Envelope - metabolism

Nuclear Lamina - metabolism

Nuclear Lamina - chemistry

Herpesvirus 1, Human - genetics

Membrane Proteins - metabolism

Capsid - metabolism

Protein-Serine-Threonine Kinases - metabolism

Details

Title: Subtitle: Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3
Creators: Natalie Leach - Department of Microbiology, The University of Iowa, 3-432 Bowen Science Building, Iowa City, IA 52242, USA
Susan L Bjerke
Desire K Christensen
Jacques M Bouchard
Fan Mou
Richard Park
Joel Baines
Tokuko Haraguchi
Richard J Roller
Resource Type: Journal article
Publication Details: Journal of virology, Vol.81(19), pp.10792-10803
DOI: 10.1128/JVI.00196-07
PMID: 17652388
PMCID: PMC2045475
NLM abbreviation: J Virol
ISSN: 0022-538X
eISSN: 1098-5514
Publisher: United States
Grant note: AI 41478 / NIAID NIH HHS R01 AI041478 / NIAID NIH HHS AI 52341 / NIAID NIH HHS R01 AI052341 / NIAID NIH HHS
Language: English
Date published: 10/2007
Academic Unit: Microbiology and Immunology
Record Identifier: 9984001132002771

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