| pubmed-article:21505419 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21505419 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:21505419 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:21505419 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:21505419 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:21505419 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:21505419 | pubmed:dateCreated | 2011-6-1 | lld:pubmed |
| pubmed-article:21505419 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21505419 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21505419 | 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. | lld:pubmed |
| pubmed-article:21505419 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21505419 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21505419 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21505419 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:21505419 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21505419 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21505419 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:21505419 | pubmed:issn | 1460-2075 | lld:pubmed |
| pubmed-article:21505419 | pubmed:author | pubmed-author:HurleyJames... | lld:pubmed |
| pubmed-article:21505419 | pubmed:author | pubmed-author:RenXuefengX | lld:pubmed |
| pubmed-article:21505419 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21505419 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:21505419 | pubmed:volume | 30 | lld:pubmed |
| pubmed-article:21505419 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21505419 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21505419 | pubmed:pagination | 2130-9 | lld:pubmed |
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| pubmed-article:21505419 | pubmed:meshHeading | pubmed-meshheading:21505419... | lld:pubmed |
| pubmed-article:21505419 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21505419 | pubmed:articleTitle | Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast. | lld:pubmed |
| pubmed-article:21505419 | pubmed:affiliation | Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA. | lld:pubmed |
| pubmed-article:21505419 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21505419 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
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