Results 11 to 20 of about 26,711 (229)
Friction Mediates Scission of Tubular Membranes Scaffolded by BAR Proteins [PDF]
Cell, 2017 International audienceMembrane scission is essential for intracellular trafficking. While BAR domain proteins such as endophilin have been reported in dynamin-independent scission of tubular membrane necks, the cutting mechanism has yet to be deciphered.
Bassereau, Patricia +12 more
core +9 more sources
Regulation of membrane scission in yeast endocytosis. [PDF]
Mol Biol Cell, 2022 Yeast N-BAR protein complex Rvs regulates scission of clathrin-coated endocytic vesicles. Rvs is recruited by its curvature-sensing BAR domain as well as curvature independently by its SH3 domain. Rvs allows invagination growth by scaffolding the membrane and thereby delaying scission. Rvs also regulates the dynamics of the endocytic actin network.
Menon D, Hummel D, Kaksonen M.
europepmc +4 more sources
Viral membrane scission. [PDF]
Annu Rev Cell Dev Biol, 2013 Virus budding is a complex, multistep process in which viral proteins make specific alterations in membrane curvature. Many different viral proteins can deform the membrane and form a budding virion, but very few can mediate membrane scission to complete the budding process.
Rossman JS, Lamb RA.
europepmc +4 more sources
Autophagosome closure requires membrane scission. [PDF]
Autophagy, 2015 During the intracellular process of macroautophagy (hereafter autophagy), a membrane-bound organelle, the autophagosome, is generated de novo. The remodeling of the autophagic membrane during the life cycle of the organelle is a complex multistep process and involves several changes in the topology of the autophagic membrane.
Knorr RL, Lipowsky R, Dimova R.
europepmc +6 more sources
Membrane scission driven by the PROPPIN Atg18. [PDF]
EMBO J, 2017 Abstract Sorting, transport, and autophagic degradation of proteins in endosomes and lysosomes, as well as the division of these organelles, depend on scission of membrane‐bound tubulo‐vesicular carriers. How scission occurs is poorly understood, but family proteins bind these membranes.
Gopaldass N +4 more
europepmc +6 more sources
Reverse-topology membrane scission by the ESCRT proteins. [PDF]
Nat Rev Mol Cell Biol, 2017 The narrow membrane necks formed during viral, exosomal and intra-endosomal budding from membranes, as well as during cytokinesis and related processes, have interiors that are contiguous with the cytosol. Severing these necks involves action from the opposite face of the membrane as occurs during the well-characterized formation of coated vesicles ...
Schöneberg J +3 more
europepmc +7 more sources
The final twist in endocytic membrane scission [PDF]
Nature Cell Biology, 2021 Many endocytic uptake events depend on the 'pinchase' activity of dynamin. By measuring the orientation of single gold nanorods, a new study reveals that invaginated clathrin-coated endocytic pits undergo a strong rotational twist prior to or concomitant with their detachment.
Johannes, Ludger, Valades-Cruz, Cesar
openaire +3 more sources
FAM134B oligomerization drives endoplasmic reticulum membrane scission for ER-phagy. [PDF]
EMBO J, 2020 Degradation of endoplasmic reticulum (ER) by selective autophagy (ER-phagy) is crucial for ER homeostasis. However, it remains unclear how ER scission is regulated for subsequent autophagosomal sequestration and lysosomal degradation. Here, we show that oligomerization of ER-phagy receptor FAM134B (also referred to as reticulophagy regulator 1 or ...
Jiang X +15 more
europepmc +4 more sources
A helical assembly of human ESCRT-I scaffolds reverse-topology membrane scission. [PDF]
Nat Struct Mol Biol, 2020 AbstractThe ESCRT complexes drive membrane scission in HIV-1 release, autophagosome closure, MVB biogenesis, cytokinesis, and other cell processes. ESCRT-I is the most upstream complex and bridges the system to HIV-1 Gag in virus release. The crystal structure of the headpiece of human ESCRT-I comprising TSG101:VPS28:VPS37B:MVB12A was determined ...
Flower TG +11 more
europepmc +8 more sources
Membrane remodeling by the M2 amphipathic helix drives influenza virus membrane scission. [PDF]
Sci Rep, 2017 AbstractMembrane scission is a crucial step in all budding processes, from endocytosis to viral budding. Many proteins have been associated with scission, though the underlying molecular details of how scission is accomplished often remain unknown. Here, we investigate the process of M2-mediated membrane scission during the budding of influenza viruses.
Martyna A +5 more
europepmc +4 more sources