Membrane Scission by the ESCRT-III Complex
By T. Wollert, Christian Wunder, Jennifer Lippincott-Schwartz, James H. Hurley. Nature, 2009
628 citations recorded by the source corpus.
The endosomal sorting complex required for transport (ESCRT) system is essential for multivesicular body biogenesis, in which cargo sorting is coupled to the invagination and scission of intralumenal vesicles. The ESCRTs are also needed for budding of enveloped viruses including human immunodeficiency virus 1, and for membrane abscission in cytokinesis. In Saccharomyces cerevisiae, ESCRT-III consists of Vps20, Snf7, Vps24 and Vps2 (also known as Did4), which assemble in that order and require the ATPase Vps4 for their disassembly. In this study, the ESCRT-III-dependent budding and scission of intralumenal vesicles into giant unilamellar vesicles was reconstituted and visualized by fluorescence microscopy. Here we show that three subunits of ESCRT-III, Vps20, Snf7 and Vps24, are sufficient to detach intralumenal vesicles. Vps2, the ESCRT-III subunit responsible for recruiting Vps4, and the ATPase activity of Vps4 were required for ESCRT-III recycling and supported additional rounds of budding. The minimum set of ESCRT-III and Vps4 proteins capable of multiple cycles of vesicle detachment corresponds to the ancient set of ESCRT proteins conserved from archaea to animals.
Subfields: Cell Biology, Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/8926c1e9c0f736f2d8c021d06759f467bae93d80
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Citations in the corpus
- The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins (2009, background): “The first in vitro reconstitution of ESCRT-III-mediated ILV budding and scission has been published recently, and shows that Vps20, Vps32 and Vps24 are sufficient for detachment of ILVs whereas Vps2 recruits Vps4 to allow recycling of these components for additional rounds of buddin”
- Analysis of ESCRT functions in exosome biogenesis, composition and secretion highlights the heterogeneity of extracellular vesicles (2013, background): “…and sequesters ubiquitylated proteins in the endosomal membrane, whereas the ESCRT-I and -II complexes appear to be responsible for membrane deformation into buds with sequestered cargo, and ESCRT-III components subsequently drive vesicle scission (Hurley and Hanson, 2010; Wollert et al., 2009).”
- Influenza Virus Assembly and Budding (2011, positive): “…ESCRT-I and -II complexes are able to modify membrane curvature and provide a scaffold for the recruitment of cargo proteins; however, addition of the ESCRT-III complex is required to mediate membrane scission and the release of the budding vesicle (Wollert and Hurley, 2010; Wollert et al., 2009).”
- The ESCRT pathway. (2011, methodology): “I, and -II complexes localize to forming ILVs, and further experiments are needed to confirm if this is true in vivo (Wollert et al., 2009).”
- Membrane budding and scission by the ESCRT machinery: it's all in the neck (2010, neutral): “, reconstitution of budding and scission in giant unilamellar vesicles ( GUVs”
- HIV-1 assembly, budding, and maturation. (2012, background): “CHMP4 subunits, possibly in complex with CHMP2 and other ESCRT-III proteins, appear to form spiraling filaments within the neck of the budding virus (Fig. 5; Ghazi-Tabatabai et al. 2008; Hanson et al. 2008; Lata et al. 2008b; Teis et al. 2008; Saksena et al. 2009; Wollert et al. 2009; Elia et al. 20”
- Phosphoinositides: tiny lipids with giant impact on cell regulation. (2013, background): “Recent studies reconstituted the assembly and lipid deforming effects of the ESCRT machinery in giant unilammellar vesicles in vitro and only found a moderate enhancement of intraluminal vesicle release by PtdIns3P or PtdIns(3,5)P2 (1723).”
- Exosomes and other extracellular vesicles in host–pathogen interactions (2014, neutral): “Through the formation of polymeric filaments mediated by ESCRT-III, membrane invagination results in ILV formation [37] (for a recent review, see [38]).”
- ESCRT Machinery Is Required for Plasma Membrane Repair (2014, background): “it ESCRT-III activity: CHMP4B is the main component of ESCRT-III filaments (33), and Vps4B DN blocks depolymerization of ESCRT subunits and therefore their recycling (3).”