ArticleThe EMBO journal2011
Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast.
Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- The green ESCRTs: Newly defined roles for ESCRT proteins in plants.The Journal of biological chemistry · 2025Review
- Article
- ESCRT-III: a versatile membrane remodeling machinery and its implications in cellular processes and diseases.Animal cells and systems · 2024Review
- Review
- EhVps23: A Component of ESCRT-I That Participates in Vesicular Trafficking and Phagocytosis ofFrontiers in cellular and infection microbiology · 2021Article
- Role of the ESCRT Pathway in Laccase Trafficking and Virulence of Cryptococcus neoformans.Infection and immunity · 2020Article
- A mechanism for protein monoubiquitination dependent on a trans-acting ubiquitin-binding domain.The Journal of biological chemistry · 2013Article
- Pkh1/2-dependent phosphorylation of Vps27 regulates ESCRT-I recruitment to endosomes.Molecular biology of the cell · 2012Article
- Experimental phasing using zinc anomalous scattering.Acta crystallographica. Section D, Biological crystallography · 2012Article
- Solution structure of the ESCRT-I and -II supercomplex: implications for membrane budding and scission.Structure (London, England : 1993) · 2012Article
- An ordered pathway for the assembly of fungal ESCRT-containing ambient pH signalling complexes at the plasma membrane.Journal of cell science · 2012Article
- Proline-rich regions and motifs in trafficking: from ESCRT interaction to viral exploitation.Traffic (Copenhagen, Denmark) · 2011Review
- How ubiquitin functions with ESCRTs.Traffic (Copenhagen, Denmark) · 2011Review
- The ESCRT machinery: from the plasma membrane to endosomes and back again.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The ESCRT-0 and ESCRT-I complexes coordinate the clustering of ubiquitinated cargo with intralumenal budding of the endosomal membrane, two essential steps in vacuolar/lysosomal protein sorting from yeast to humans. The 1.85-Å crystal structure of interacting regions of the yeast ESCRT-0 and ESCRT-I complexes reveals that PSDP motifs of the Vps27 ESCRT-0 subunit bind to a novel electropositive N-terminal site on the UEV domain of the ESCRT-I subunit Vps23 centred on Trp16. This novel site is completely different from the C-terminal part of the human UEV domain that binds to P(S/T)AP motifs of human ESCRT-0 and HIV-1 Gag. Disruption of the novel PSDP-binding site eliminates the interaction in vitro and blocks enrichment of Vps23 in endosome-related class E compartments in yeast cells. However, this site is non-essential for sorting of the ESCRT cargo Cps1. Taken together, these results show how a conserved motif/domain pair can evolve to use strikingly different binding modes in different organisms.
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