Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body.

By M. Babst, David J. Katzmann, W. B. Snyder, Beverly Wendland, S. Emr. Developmental Cell, 2002

667 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/cd138d820b773da7ecc5399c226bd70cd330213d

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Citations in the corpus

Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. (2002, neutral): “Vps4 assembles into an AAA-type ATPase, which catalyzes the release of other HA as well as both Vps24 and Snf7 were found in the soluble cytoplasmic fraction (Figure 2A, lanes 1 and 2, class E Vps proteins from the endosomal membrane (Babst et al., 1997, 1998, 2002).”
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).”
The protein network of HIV budding. (2003, background): “Firstly, we and others often human CHMP6 appears to be recruited by the ESCRTobserved a thickening of the cytoplasmic faces of mem- II complex, whereas the CHMP4 proteins are recruited branes near sites of virus budding, which may corre- by AIP1 (see Figures 1 and 7) (Babst et al., 2002b; Odospond t”
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).”
Exosomes and other extracellular vesicles in host–pathogen interactions (2014, positive): “ESCRT-0 subsequently recruits ESCRT-1 to the endosomal membrane, which in turn recruits the remaining members of the ESCRT machinery, ESCRT-II and ESCRT-III [35,36].”
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).”
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).”