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Dissociation of heterochromatin protein 1 from lamin B receptor induced by human polyomavirus agnoprotein: role in nuclear egress of viral particles
Author(s) -
Okada Yuki,
Suzuki Tadaki,
Sunden Yuji,
Orba Yasuko,
Kose Shingo,
Imamoto Naoko,
Takahashi Hidehiro,
Tanaka Shinya,
Hall William W,
Nagashima Kazuo,
Sawa Hirofumi
Publication year - 2005
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400406
Subject(s) - lamin , inner membrane , nuclear pore , cell nucleus , microbiology and biotechnology , biology , nuclear transport , fluorescence recovery after photobleaching , nuclear lamina , nuclear localization sequence , nucleolus , cytoplasm , nuclear protein , viral envelope , nucleus , gene , genetics , transcription factor , membrane , glycoprotein , mitochondrion
The nuclear envelope is one of the chief obstacles to the translocation of macromolecules that are larger than the diameter of nuclear pores. Heterochromatin protein 1 (HP1) bound to the lamin B receptor (LBR) is thought to contribute to reassembly of the nuclear envelope after cell division. Human polyomavirus agnoprotein (Agno) has been shown to bind to HP1α and to induce its dissociation from LBR, resulting in destabilization of the nuclear envelope. Fluorescence recovery after photobleaching showed that Agno increased the lateral mobility of LBR in the inner nuclear membrane. Biochemical and immunofluorescence analyses showed that Agno is targeted to the nuclear envelope and facilitates the nuclear egress of polyomavirus‐like particles. These results indicate that dissociation of HP1α from LBR and consequent perturbation of the nuclear envelope induced by polyomavirus Agno promote the translocation of virions out of the nucleus.