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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.
Highlights
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
Super-resolution imaging and line plot measurements showed that punctate structures with CHMP4BEGFP were associated with lamin A/C, but not with the endoplasmic reticulum (ER) integral protein calnexin, which is localized at the outer nuclear membrane (ONM) and ER18 (Fig. 1d)
nuclear egress complex (NEC) have intrinsic capabilities to remodel membranes, it is not known whether NECs themselves sufficiently carry out herpesvirus primary envelopment in herpesvirus-infected cells
Summary
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. ALIX and/or ESCRT-I are known to bind regulators in various pathwayspecific signals mediated by the ESCRT-III machinery: these interactions are required to recruit ESCRT-III proteins to their sites of action[8] These regulators include ubiquitin for multivesicular body (MVB) formation, CEP55 for cytokinesis, and GAG p6 for human immunodeficiency virus 1 (HIV-1) budding[8]. We present data showing ESCRT-III downregulates INM proliferation in uninfected human cells These results identify functions of ESCRT-III in the vesicle-mediated nucleocytoplasmic transport of HSV-1 and in the regulation of INM integrity in uninfected cells
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