RT Journal Article SR Electronic T1 LEM2 and CHMP7 function in ESCRT-dependent nuclear envelope closure in yeast and human cells JF bioRxiv FD Cold Spring Harbor Laboratory SP 049312 DO 10.1101/049312 A1 Mingyu Gu A1 Opal S. Chen A1 Dollie Lajoie A1 Mark S. Ladinsky A1 Michael J. Redd A1 Linda Nikolova A1 Pamela J. Bjorkman A1 Katharine S. Ullman A1 Wesley I. Sundquist A1 Adam Frost YR 2016 UL http://biorxiv.org/content/early/2016/04/19/049312.abstract 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.