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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2011-6-1
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1460-2075
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2130-9
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pubmed:meshHeading |
pubmed-meshheading:21505419-Amino Acid Motifs,
pubmed-meshheading:21505419-Amino Acid Sequence,
pubmed-meshheading:21505419-Carboxypeptidases,
pubmed-meshheading:21505419-Crystallography, X-Ray,
pubmed-meshheading:21505419-Endosomal Sorting Complexes Required for Transport,
pubmed-meshheading:21505419-Endosomes,
pubmed-meshheading:21505419-Models, Molecular,
pubmed-meshheading:21505419-Molecular Sequence Data,
pubmed-meshheading:21505419-Mutagenesis,
pubmed-meshheading:21505419-Mutant Proteins,
pubmed-meshheading:21505419-Protein Binding,
pubmed-meshheading:21505419-Protein Interaction Domains and Motifs,
pubmed-meshheading:21505419-Protein Structure, Quaternary,
pubmed-meshheading:21505419-Saccharomyces cerevisiae,
pubmed-meshheading:21505419-Saccharomyces cerevisiae Proteins
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pubmed:year |
2011
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pubmed:articleTitle |
Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast.
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pubmed:affiliation |
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Intramural
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