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• W2339688002 abstract "Abstract Mechanisms that ensure the integrity of the nuclear envelope rely on membrane remodeling proteins like the ESCRTs and the AAA ATPase Vps4, which help seal the nuclear envelope at the end of mitosis and prevent the formation of defective nuclear pore complexes (NPCs). Here, we show that the integral inner nuclear membrane proteins Heh1 and Heh2 directly bind the ESCRT-III, Snf7, and the ESCRT-II/III chimera, Chm7, in their ‘open’ forms. Moreover, Heh1 is required for Chm7-recruitment to the nuclear envelope. As Chm7 accumulates on the nuclear envelope upon blocks to NPC assembly, but not to nuclear transport, interactions between ESCRTs and the Heh proteins might form a biochemically distinct nuclear envelope subdomain that delimits regions of assembling NPCs. Interestingly, deletion of CHM7 suppresses the formation of the storage of improperly assembled NPC compartment prevalent in vps4Δ strains. Thus, our data support that the Heh1-dependent recruitment of Chm7 is a key component of a quality control pathway whose local regulation by Vps4 and the transmembrane nup, Pom152, prevents loss of nuclear compartmentalization by defective NPCs." @default.
• W2339688002 created "2016-06-24" @default.
• W2339688002 creator A5029484180 @default.
• W2339688002 creator A5040283216 @default.
• W2339688002 creator A5048661647 @default.
• W2339688002 creator A5063279981 @default.
• W2339688002 creator A5073749793 @default.
• W2339688002 date "2016-04-18" @default.
• W2339688002 modified "2023-09-26" @default.
• W2339688002 title "Chm7 and Heh1 form a nuclear envelope subdomain for nuclear pore complex quality control" @default.
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