ESCRT-III mediates budding across the inner nuclear membrane and regulates its integrity
Jun Arii,
Mizuki Watanabe,
Fumio Maeda,
Noriko Tokai-Nishizumi,
Takahiro Chihara,
Masayuki Miura,
Yuhei Maruzuru,
Naoto Koyanagi,
Akihisa Kato and
Yasushi Kawaguchi ()
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Jun Arii: The Institute of Medical Science, The University of Tokyo, Minato-ku
Mizuki Watanabe: The Institute of Medical Science, The University of Tokyo, Minato-ku
Fumio Maeda: The Institute of Medical Science, The University of Tokyo, Minato-ku
Noriko Tokai-Nishizumi: The Institute of Medical Science, The University of Tokyo, Minato-ku
Takahiro Chihara: The University of Tokyo
Masayuki Miura: The University of Tokyo
Yuhei Maruzuru: The Institute of Medical Science, The University of Tokyo, Minato-ku
Naoto Koyanagi: The Institute of Medical Science, The University of Tokyo, Minato-ku
Akihisa Kato: The Institute of Medical Science, The University of Tokyo, Minato-ku
Yasushi Kawaguchi: The Institute of Medical Science, The University of Tokyo, Minato-ku
Nature Communications, 2018, vol. 9, issue 1, 1-15
Abstract:
Abstract Vesicle-mediated nucleocytoplasmic transport is a nuclear pore-independent mechanism for the nuclear export of macromolecular complexes, but the molecular basis for this transport remains largely unknown. Here we show that endosomal sorting complex required for transport-III (ESCRT-III) is recruited to the inner nuclear membrane (INM) during the nuclear export of herpes simplex virus 1 (HSV-1). Scission during HSV-1 budding through the INM is prevented by depletion of ESCRT-III proteins. Interestingly, in uninfected human cells, the depletion of ESCRT-III proteins induces aberrant INM proliferation. Our results show that HSV-1 expropriates the ESCRT-III machinery in infected cells for scission of the INM to produce vesicles containing progeny virus nucleocapsids. In uninfected cells, ESCRT-III regulates INM integrity by downregulating excess INM.
Date: 2018
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05889-9
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DOI: 10.1038/s41467-018-05889-9
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