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Science 2 August 2002:
Vol. 297. no. 5582, pp. 854 - 857
DOI: 10.1126/science.1071506
Prev | Table of Contents

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. Koszinowski1dagger

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.

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.

dagger    To whom correspondence should be addressed. E-mail: koszinowski{at}m3401.mpk.med.uni-muenchen.de

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Science. ISSN 0036-8075 (print), 1095-9203 (online)