Herpes Simplex Virus Type 1 Infection Induces Activation and Recruitment of Protein Kinase C to the Nuclear Membrane and Increased Phosphorylation of Lamin B
Open Access
- 1 January 2006
- journal article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 80 (1), 494-504
- https://doi.org/10.1128/jvi.80.1.494-504.2006
Abstract
We report that herpes simplex virus type 1 (HSV-1) infection leads to the recruitment of protein kinase C (PKC) to the nuclear rim. In HEp-2 cells, PKC recruitment to the nuclear rim was initiated between 8 h and 12 h postinfection. PKCδ, a proapoptotic kinase, was completely recruited to the nuclear rim upon infection with HSV-1. PKCα was less dramatically relocalized mostly at the nuclear rim upon infection, although some PKCα remained in the cytoplasm. PKCζ-specific immunofluorescence was not significantly relocated to the nuclear rim. The U L 34 and U L 31 proteins, as well as their association, were each required for PKC recruitment to the nuclear rim. The HSV-1 U S 3 protein product, a kinase which regulates the phosphorylation state and localization of U L 34, was not required for PKC recruitment to the nuclear rim; however, it was required for proper localization along the nuclear rim, as PKC appeared unevenly distributed along the nuclear rim of cells infected with U S 3 null and kinase-dead mutants. HSV-1 infection induced the phosphorylation of both lamin B and PKC. Elevated lamin B phosphorylation in HSV-1-infected cells was partially reduced by inhibitors of PKC. The data suggest a model in which kinases that normally disassemble the nuclear lamina during apoptosis are recruited to the nuclear membrane through functions requiring U L 31 and U L 34. We hypothesize that the recruitment of PKC functions to phosphorylate lamin B to help modify the nuclear lamina and promote budding of nucleocapsids at the inner nuclear membrane.This publication has 33 references indexed in Scilit:
- Characterization and Intracellular Localization of the Epstein-Barr Virus Protein BFLF2: Interactions with BFRF1 and with the Nuclear LaminaJournal of Virology, 2005
- BFRF1 of Epstein-Barr Virus Is Essential for Efficient Primary Viral Envelopment and EgressJournal of Virology, 2005
- The nuclear lamina comes of ageNature Reviews Molecular Cell Biology, 2005
- Comprehensive Mutational Analysis of a Herpesvirus Gene in the Viral Genome Context Reveals a Region Essential for Virus ReplicationJournal of Virology, 2004
- Effects of Charged Cluster Mutations on the Function of Herpes Simplex Virus Type 1 U L 34 ProteinJournal of Virology, 2003
- Molecular characterization of protein kinase C‐α binding to lamin AJournal of Cellular Biochemistry, 2002
- Fate of the Inner Nuclear Membrane Protein Lamin B Receptor and Nuclear Lamins in Herpes Simplex Virus Type 1 InfectionJournal of Virology, 2001
- Lamin B Phosphorylation by Protein Kinase Cα and Proteolysis during Apoptosis in Human Leukemia HL60 CellsOnline Journal of Public Health Informatics, 1998
- Two Different Proteases Are Involved in the Proteolysis of Lamin during ApoptosisBiochemical and Biophysical Research Communications, 1997
- Characterization of Herpes Simplex Virus Strains Differing in their Effects on Social Behaviour of Infected CellsJournal of General Virology, 1968