The endosomal sorting complexes required for transport (ESCRT) are best known for their role in sorting ubiquitylated membrane proteins into endosomes. The most ancient component of the ESCRT machinery is ESCRT-III, which is capable of oligomerizing into a helical filament that drives the invagination and scission of membranes aided by the AAA ATPase, Vps4, in several additional subcellular contexts. Our recent study broadens the work of ESCRT-III by identifying its role in a quality control pathway at the nuclear envelope (NE) that ensures the normal biogenesis of nuclear pore complexes (NPCs). Here, we will elaborate on how we envision this mechanism to progress and incorporate ESCRT-III into an emerging model of nuclear pore formation. Moreover, we speculate there are additional roles for the ESCRT-III machinery at the NE that broadly function to ensure its integrity and the maintenance of the nuclear compartment.
Spatial perspectives in the redox code-Mass spectrometric proteomics studies of moonlighting proteins
Chm7 and Heh1 collaborate to link nuclear pore complex quality control with nuclear envelope sealing
A temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic
Nuclear transport defects and nuclear envelope alterations are associated with mutation of the Saccharomyces cerevisiae NPL4 gene
A yeast acetyl coenzyme A carboxylase mutant links very-long-chain fatty acid synthesis to the structure and function of the nuclear membrane-pore complex
GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function
The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies
Karyopherins in nuclear pore biogenesis: a role for Kap121p in the assembly of Nup53p into nuclear pore complexes
The yeast integral membrane protein Apq12 potentially links membrane dynamics to assembly of nuclear pore complexes
Inner/Outer nuclear membrane fusion in nuclear pore assembly: biochemical demonstration and molecular analysis
Localization of Pom121 to the inner nuclear membrane is required for an early step of interphase nuclear pore complex assembly
Repetitive disruptions of the nuclear envelope invoke temporary loss of cellular compartmentalization in laminopathies
A dominant-negative form of POM121 binds chromatin and disrupts the two separate modes of nuclear pore assembly
Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling
The ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr Virus
Coordinated binding of Vps4 to ESCRT-III drives membrane neck constriction during MVB vesicle formation
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