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Science 2 August 2002: Vol. 297. no. 5582, pp. 854 - 857 DOI: 10.1126/science.1071506
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Reports
Cytomegalovirus Recruitment of Cellular Kinases to Dissolve the Nuclear Lamina
Walter Muranyi,1*
Jürgen Haas,1
Markus Wagner,1
Georg Krohne,2
Ulrich H. Koszinowski1
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 -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.
1 Genzentrum and Max-von-Pettenkofer
Institut, Ludwig-Maximilians-Universität München, 80336 München, Germany.
2 Division of Electron
Microscopy, Biocenter of the University of Würzburg, 97074 Würzburg, Germany.
*
Present address: Abteilung Virologie, Hygiene-Institut,
Ruprecht-Karls-Universität Heidelberg, 69120 Heidelberg, Germany.
To whom correspondence should be addressed.
E-mail: koszinowski{at}m3401.mpk.med.uni-muenchen.de
Read the Full Text
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