Apr 19, 2016

LEM2 and CHMP7 function in ESCRT-dependent nuclear envelope closure in yeast and human cells

BioRxiv : the Preprint Server for Biology
Mingyu GuKatharine S Ullman


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 lem2 or 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.

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Mentioned in this Paper

Inner Nuclear Membrane
VPS4A protein, human
TMPO gene
Biochemical Pathway
Carboxy-Terminal Amino Acid
Reparative Closure
Adenosine Triphosphatases
Binding Sites, Antibody
Complex (molecular entity)
Cell Division

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