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Cytomegalovirus Recruitment of Cellular Kinases to Dissolve the Nuclear Lamina

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Science  02 Aug 2002:
Vol. 297, Issue 5582, pp. 854-857
DOI: 10.1126/science.1071506

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Abstract

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.

  • * 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

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