Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast
Copyright policy )Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast
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.
- National Institute of Health Pakistan
- National Institute of Diabetes and Digestive and Kidney Diseases United States
- National Institutes of Health United States
Models, Molecular, Saccharomyces cerevisiae Proteins, Endosomal Sorting Complexes Required for Transport, Amino Acid Motifs, Molecular Sequence Data, Carboxypeptidases, Endosomes, Saccharomyces cerevisiae, Crystallography, X-Ray, Mutagenesis, Mutant Proteins, Protein Interaction Domains and Motifs, Amino Acid Sequence, Protein Structure, Quaternary, Protein Binding
Models, Molecular, Saccharomyces cerevisiae Proteins, Endosomal Sorting Complexes Required for Transport, Amino Acid Motifs, Molecular Sequence Data, Carboxypeptidases, Endosomes, Saccharomyces cerevisiae, Crystallography, X-Ray, Mutagenesis, Mutant Proteins, Protein Interaction Domains and Motifs, Amino Acid Sequence, Protein Structure, Quaternary, Protein Binding
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