PT  - JOURNAL ARTICLE
AU  - Mingyu Gu
AU  - Opal S. Chen
AU  - Dollie Lajoie
AU  - Mark S. Ladinsky
AU  - Michael J. Redd
AU  - Linda Nikolova
AU  - Pamela J. Bjorkman
AU  - Katharine S. Ullman
AU  - Wesley I. Sundquist
AU  - Adam Frost
TI  - LEM2 and CHMP7 function in ESCRT-dependent nuclear envelope closure in yeast and human cells
AID  - 10.1101/049312
DP  - 2016 Jan 01
TA  - bioRxiv
PG  - 049312
4099  - http://biorxiv.org/content/early/2016/04/19/049312.short
4100  - http://biorxiv.org/content/early/2016/04/19/049312.full
AB  - ESCRT-III proteins have been implicated in sealing the nuclear envelope in mammals, spindle pole body dynamics in fission yeast, and the clearance of defective nuclear pore complexes in budding yeast. Here, we report that Lem2p (LEM2), a member of the LEM (Lap2-Emerin-Man1) family of inner nuclear membrane proteins, and the ESCRT-II/ESCRT-III hybrid protein Cmp7p (CHMP7), collaborate to recruit ESCRT-III proteins to holes in the nuclear membrane. In fission yeast, deletion of the ATPase vps4 leads to severe defects in nuclear morphology and integrity. These phenotypes are suppressed by loss-of-function mutations that arise spontaneously in lem2or cmp7, implying that all three function in the same pathway. In mammals, ESCRT factors participate in nuclear envelope reformation in anaphase, and we show that this process similarly depends on both LEM2 and CHMP7. Our observations suggest that Lem2p/LEM2 acts as a site-specific adaptor that recruits Cmp7p/CHMP7 and other ESCRT factors to the nuclear envelope.