| Literature DB >> 34578469 |
Kevin M Rose1, Stephanie J Spada2, Vanessa M Hirsch2, Fadila Bouamr2.
Abstract
The authors wish to make the following erratum to this paper [...].Entities:
Year: 2021 PMID: 34578469 PMCID: PMC8472907 DOI: 10.3390/v13091705
Source DB: PubMed Journal: Viruses ISSN: 1999-4915 Impact factor: 5.048
Figure 1The respective roles of ALIX and ESCRT-I in the sorting of membranous cargo. Upon internalization, ubiquitylated cargo is detected by ALIX (left) and ESCRT-I (right) for compartmentalization into intraluminal vesicles that are destined for degradation via the late endosome. Both ALIX and ESCRT-I contain ubiquitin binding domains that facilitate this first step. Unlike ESCRT-I, ALIX possesses an ESCRT-III binding domain that allows for the direct recruitment of ESCRT-III and VPS4, the machinery required for sealing of cargo within intraluminal vesicles and abscising these vesicles from the endosomal membrane. In a similar fashion, the ESCRT-I component TSG101 binds ubiquitylated cargo, while the VPS28 component can recruit ESCRT-III through ESCRT-II which also binds ubiquitylated cargo as well as phospho-inositol lipids.