Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting.
By M. Babst, David J. Katzmann, Eden J Estepa-Sabal, T. Meerloo, S. Emr. Developmental Cell, 2002
891 citations recorded by the source corpus.
The sorting of transmembrane proteins (e.g., cell surface receptors) into the multivesicular body (MVB) pathway to the lysosomal/vacuolar lumen requires the function of the ESCRT protein complexes. The soluble coiled-coil-containing proteins Vps2, Vps20, Vps24, and Snf7 are recruited from the cytoplasm to endosomal membranes where they oligomerize into a protein complex, ESCRT-III. ESCRT-III contains two functionally distinct subcomplexes. The Vps20-Snf7 subcomplex binds to the endosomal membrane, in part via the myristoyl group of Vps20. The Vps2-Vps24 subcomplex binds to the Vps20-Snf7 complex and thereby serves to recruit additional cofactors to this site of protein sorting. We provide evidence for a role for ESCRT-III in sorting and/or concentration of MVB cargoes.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/c4333ba416735bfa89159c82bc62669ade7ba83a
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In Cell Biology
- T. Balla
- Harald A. Stenmark
- Robert C. Piper
- David J. Katzmann
- S. Emr
- Michael Zhuo Wang
- W. Henne
- Nicholas J. Buchkovich
In Molecular Biology
- T. Balla
- Harald A. Stenmark
- David J. Katzmann
- Robert C. Piper
- Michael Zhuo Wang
- W. Henne
- Wesley I. Sundquist
- Nicholas J. Buchkovich
Citations in the corpus
- The ESCRT pathway. (2011, background): “This is supported by in vitro reconstitution of ESCRT-III assembly where membrane depressions were observed on liposomes when purified Vps20, Snf7, Vps24, and Vps2 were added in a ratio of 1:10:5:3 but not seen when individual subunits were left out (Saksena et al., 2009).”
- Multivesicular Endosome Biogenesis in the Absence of ESCRTs (2009, background): “It has been established that upon depletion of either of the subunits of the ESCRTs, the complex loses its integrity and that the expression levels of the other subunits are decreased (14,17,24,31).”
- Biogenesis and function of multivesicular bodies. (2007, background): “If such a supercomplex exists in vivo, it likely forms on membranes because biochemical analysis of soluble fractions finds ESCRTI and ESCRT-II as discrete complexes (Babst et al. 2002b, Katzmann et al. 2001).”
- Overview of Extracellular Vesicles, Their Origin, Composition, Purpose, and Methods for Exosome Isolation and Analysis (2019, background): “The regulation of MVB and exosome formation and release is through the endosomal sorting complexes required for transport (ESCRT) pathway [44,45].”
- AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. (2003, background): “Vps32 is a component of ESCRT-III, and Vps4 recycles ESCRT complexes (Babst et al., 2002a).”
- Phosphoinositides: tiny lipids with giant impact on cell regulation. (2013, background): “Vps34p is also important for the membrane invaginations in multivesicular bodies (MVB) (70, 71, 765) and for various forms of autophagy (779).”
- Biogenesis of extracellular vesicles (EV): exosomes, microvesicles, retrovirus-like vesicles, and apoptotic bodies (2013, neutral): “There are four multi-protein complexes required for ILV formation and they are termed ESCRT 0, I, II, and III [39–41].”
- Introduction to Extracellular Vesicles: Biogenesis, RNA Cargo Selection, Content, Release, and Uptake (2016, neutral): “It has been suggested that ESCRT I and II are the initiators and drivers of the intraluminal membrane budding, whereas ESCRT III completes this process (Babst et al. 2002; Henne et al. 2013).”