Science (American Association for the Advancement of Science), 2002-08, Vol.297 (5582), p.854-857
2002
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Details
- Autor(en) / Beteiligte
- Titel
- Cytomegalovirus Recruitment of Cellular Kinases to Dissolve the Nuclear Lamina
- Ist Teil von
- Science (American Association for the Advancement of Science), 2002-08, Vol.297 (5582), p.854-857
- Ort / Verlag
- Washington, DC: American Association for the Advancement of Science
- Erscheinungsjahr
- 2002
- Quelle
- American Association for the Advancement of Science
- Beschreibungen/Notizen
- The passage of large-sized herpesviral capsids through the nuclear lamina and the inner nuclear membrane to leave the nucleus requires a dissolution of the nuclear lamina. Here, we report on the functions of M50/p35, a β-herpesviral protein of murine cytomegalovirus. M50/p35 inserts into the inner nuclear membrane and is aggregated by a second viral protein, M53/p38, to form the capsid docking site. M50/p35 recruits the cellular protein kinase C for phosphorylation and dissolution of the nuclear lamina, suggesting that herpesviruses target a critical element of nuclear architecture.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0036-8075eISSN: 1095-9203DOI: 10.1126/science.1071506Titel-ID: cdi_proquest_miscellaneous_743158396
- Format
- –
- Schlagworte
- 3T3 cells, Analysis, Antibodies, Biological and medical sciences, Capsid, Capsid - metabolism, Cell Line, Cellular biology, Cellular immunity, Cytomegalovirus, Cytomegaloviruses, Fundamental and applied biological sciences. Psychology, Herpes viruses, Humans, Infections, Lamins, Medical research, Medicine, Experimental, Microbiology, Mitosis, Morphogenesis, Movement, Muromegalovirus - genetics, Muromegalovirus - physiology, Nuclear Envelope - chemistry, Nuclear Envelope - enzymology, Nuclear Envelope - metabolism, Nuclear Envelope - virology, Nuclear Proteins - metabolism, Nucleoproteins, Open Reading Frames - genetics, Phenotypes, Phosphorylation, Protein Binding, Protein Kinase C - metabolism, Proteins, Recruitment, Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains, Viral proteins, Viral Proteins - genetics, Viral Proteins - metabolism, Virology, Virus Assembly