RT Journal Article
T1 ESCRT-III controls nuclear envelope reformation
A1 Olmos Buchelt, Yolanda
A1 Hodgson, Lorna
A1 Mantell, Judith
A1 Verkade, Paul
A1 Carlton, Jeremy G.
AB During telophase, the nuclear envelope (NE) reforms around daughter nuclei to ensure proper segregation of nuclear and cytoplasmic contents. NE reformation requires the coating of chromatin by membrane derived from the endoplasmic reticulum, and a subsequent annular fusion step to ensure that the formed envelope is sealed. How annular fusion is accomplished is unknown, but it is thought to involve the p97 AAA-ATPase complex and bears a topological equivalence to the membrane fusion event that occurs during the abscission phase of cytokinesis. Here we show that the endosomal sorting complex required for transport-III (ESCRT-III) machinery localizes to sites of annular fusion in the forming NE in human cells, and is necessary for proper post-mitotic nucleo-cytoplasmic compartmentalization. The ESCRT-III component charged multivesicular body protein 2A (CHMP2A) is directed to the forming NE through binding to CHMP4B, and provides an activity essential for NE reformation. Localization also requires the p97 complex member ubiquitin fusion and degradation 1 (UFD1). Our results describe a novel role for the ESCRT machinery in cell division and demonstrate a conservation of the machineries involved in topologically equivalent mitotic membrane remodelling events.
PB Macmillan
SN 0028-0836
YR 2015
FD 2015-06-03
LK https://hdl.handle.net/20.500.14352/105053
UL https://hdl.handle.net/20.500.14352/105053
LA eng
NO Olmos Y, Hodgson L, Mantell J, Verkade P, Carlton JG. ESCRT-III controls nuclear envelope reformation. Nature. 2015;522(7555):236-9.
DS Docta Complutense
RD 6 abr 2025