Cellular p32 recruits cytomegalovirus kinase pUL97 to redistribute the nuclear lamina
| Autor: | Ramona Jochmann, Manfred Marschall, Andrea Marzi, Martina Leis, Peter Lischka, Patricia aus dem Siepen, Martina Kalmer, Sabrina Auerochs, Thomas Stamminger |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
viruses
Green Fluorescent Proteins Cytomegalovirus Lamin B receptor Biology Virus Replication Biochemistry Cell Line Mitochondrial Proteins Viral entry Two-Hybrid System Techniques Viral structural protein medicine Humans Nuclear membrane Phosphorylation Nuclear export signal Fluorescent Antibody Technique Indirect Molecular Biology Cells Cultured Skin Cell Nucleus Nuclear Lamina Cell Biology Fibroblasts Molecular biology Clone Cells body regions Phosphotransferases (Alcohol Group Acceptor) medicine.anatomical_structure Viral replication Nuclear lamina Carrier Proteins Lamin HeLa Cells |
| Zdroj: | The Journal of biological chemistry. 280(39) |
| ISSN: | 0021-9258 |
| Popis: | Replication of human cytomegalovirus is limited at the level of nucleocytoplasmic transport of viral capsids, a process that requires the disassembly of the nuclear lamina. Deletion of the protein kinase gene UL97 from the viral genome showed that the activity of pUL97 plays an important role for viral capsid egress. Here, we report that p32, a novel cellular interactor of the viral kinase pUL97, promotes the accumulation of pUL97 at the nuclear membrane by recruiting the p32-pUL97 complex to the lamin B receptor. Transfection of active pUL97, but not a catalytically inactive mutant, induced a redistribution of lamina components as demonstrated for recombinant lamin B receptor-green fluorescent protein and endogenous lamins A and C. Consistent with this, p32 itself and lamins were phosphorylated by pUL97. Importantly, overexpression of p32 in human cytomegalovirus-infected cells resulted in increased efficiency of viral replication and release of viral particles. Thus, it is highly suggestive that the cellular protein p32 recruits pUL97 to induce a dissolution of the nuclear lamina thereby facilitating the nuclear export of viral capsids. |
| Databáze: | OpenAIRE |
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