Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina.
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 beta-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.
Muranyi
Walter
W
Genzentrum and Max-von-Pettenkofer Institut, Ludwig-Maximilians-Universität München, 80336 München, Germany.
Haas
Jürgen
J
Wagner
Markus
M
Krohne
Georg
G
Koszinowski
Ulrich H
UH
D002213:Capsid / Q000378:metabolism; D002460:Cell Line; D006801:Humans; D034882:Lamins; D009068:Movement; D018146:Muromegalovirus / Q000235:genetics / Q000502:physiology*; D009685:Nuclear Envelope / Q000737:chemistry / Q000201:enzymology / Q000378:metabolism* / Q000821:virology*; D009687:Nuclear Proteins / Q000378:metabolism; D016366:Open Reading Frames / Q000235:genetics; D010766:Phosphorylation; D011485:Protein Binding; D011493:Protein Kinase C / Q000378:metabolism*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism; D019065:Virus Assembly
D034882:Lamins; D009687:Nuclear Proteins; D014764:Viral Proteins; D011493:Protein Kinase C