pubmed-article:19531583 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19531583 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
pubmed-article:19531583 | lifeskim:mentions | umls-concept:C0751984 | lld:lifeskim |
pubmed-article:19531583 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
pubmed-article:19531583 | lifeskim:mentions | umls-concept:C1426057 | lld:lifeskim |
pubmed-article:19531583 | lifeskim:mentions | umls-concept:C1826758 | lld:lifeskim |
pubmed-article:19531583 | pubmed:issue | Pt 14 | lld:pubmed |
pubmed-article:19531583 | pubmed:dateCreated | 2009-7-2 | lld:pubmed |
pubmed-article:19531583 | pubmed:abstractText | Retromer is a membrane-associated heteropentameric coat complex that functions in the endosome-to-Golgi retrieval of the cation-independent mannose-6-phosphate receptor, the Wntless protein and other membrane proteins of physiological significance. Retromer comprises two functional subcomplexes: the cargo-selective subcomplex is a trimer of the VPS35, VPS29, VPS26 proteins, whereas the sorting nexin proteins, Snx1 and Snx2 function to tubulate the endosomal membrane. Unlike the sorting nexins, which contain PtdIns3P-binding PX domains, the cargo-selective VPS35/29/26 complex has no lipid-binding domains and its recruitment to the endosomal membrane remains mechanistically uncharacterised. In this study we show that the VPS35/29/26 complex interacts with the small GTPase Rab7 and requires Rab7 for its recruitment to the endosome. We show that the Rab7K157N mutant that causes the peripheral neuropathy, Charcot-Marie-Tooth disease, does not interact with the VPS35/29/26 complex, resulting in a weakened association with the membrane. We have also identified a novel retromer-interacting protein, TBC1D5, which is a member of the Rab GAP family of proteins that negatively regulates VPS35/29/26 recruitment and causes Rab7 to dissociate from the membrane. We therefore propose that recruitment of the cargo-selective VPS35/29/26 complex is catalysed by Rab7 and inhibited by the Rab-GAP protein, TBC1D5. | lld:pubmed |
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pubmed-article:19531583 | pubmed:language | eng | lld:pubmed |
pubmed-article:19531583 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19531583 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19531583 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:19531583 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19531583 | pubmed:month | Jul | lld:pubmed |
pubmed-article:19531583 | pubmed:issn | 0021-9533 | lld:pubmed |
pubmed-article:19531583 | pubmed:author | pubmed-author:SeamanMatthew... | lld:pubmed |
pubmed-article:19531583 | pubmed:author | pubmed-author:BrightNichola... | lld:pubmed |
pubmed-article:19531583 | pubmed:author | pubmed-author:HarbourMichae... | lld:pubmed |
pubmed-article:19531583 | pubmed:author | pubmed-author:TattersallDan... | lld:pubmed |
pubmed-article:19531583 | pubmed:author | pubmed-author:ReadEliotE | lld:pubmed |
pubmed-article:19531583 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:19531583 | pubmed:day | 15 | lld:pubmed |
pubmed-article:19531583 | pubmed:volume | 122 | lld:pubmed |
pubmed-article:19531583 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19531583 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19531583 | pubmed:pagination | 2371-82 | lld:pubmed |
pubmed-article:19531583 | pubmed:dateRevised | 2010-9-24 | lld:pubmed |
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