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ESCRT-III mediates budding across the inner nuclear membrane and regulates its integrity.


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.

SUBMITTER: Arii J 

PROVIDER: S-EPMC6107581 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature

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ESCRT-III mediates budding across the inner nuclear membrane and regulates its integrity.

Arii Jun J   Watanabe Mizuki M   Maeda Fumio F   Tokai-Nishizumi Noriko N   Chihara Takahiro T   Miura Masayuki M   Maruzuru Yuhei Y   Koyanagi Naoto N   Kato Akihisa A   Kawaguchi Yasushi Y  

Nature communications 20180823 1


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. Interes  ...[more]

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