| pubmed-article:17892535 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17892535 | lifeskim:mentions | umls-concept:C0037420 | lld:lifeskim |
| pubmed-article:17892535 | lifeskim:mentions | umls-concept:C1325734 | lld:lifeskim |
| pubmed-article:17892535 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17892535 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:17892535 | lifeskim:mentions | umls-concept:C2348519 | lld:lifeskim |
| pubmed-article:17892535 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:17892535 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:17892535 | pubmed:dateCreated | 2007-11-12 | lld:pubmed |
| pubmed-article:17892535 | pubmed:abstractText | The penta-subunit retromer complex of yeast mediates selective retrieval of membrane proteins from the prevacuolar endosome to the trans Golgi network. In this study, we set out to generate a panel of vps35 dominant-negative mutants that disrupt retromer-mediated cargo sorting. Mapping of the mutations revealed two types of alterations leading to dominant-negative behavior of the 944-amino acid protein: (i) mutations at or near the R(98) residue or (ii) C-terminal truncations exemplified by a nonsense mutation at codon 733. Both could be suppressed by overexpression of wild-type Vps35p, suggesting that these dominant-negative mutants compete for interactions with other retromer subunits. Interestingly, Vps35-R(98)W expression destabilized Vps26p while having no effect on Vps29p stability, while Vps35-Q(733)* expression affected Vps29p stability but had no effect on Vps26p. Measurement of Vps35/Vps26 and Vps35/Vps29 pairwise associations by coimmunoprecipitation in the presence or absence of other retromer subunits indicated that the R(98) residue, which is part of a conserved PRLYL motif, is critical for Vps35p binding to Vps26p, while both R(98) and residues 733-944 are needed for efficient binding to Vps29p. | lld:pubmed |
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| pubmed-article:17892535 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:17892535 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17892535 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:17892535 | pubmed:issn | 1398-9219 | lld:pubmed |
| pubmed-article:17892535 | pubmed:author | pubmed-author:ArvanPeterP | lld:pubmed |
| pubmed-article:17892535 | pubmed:author | pubmed-author:ZhaoXiangX | lld:pubmed |
| pubmed-article:17892535 | pubmed:author | pubmed-author:ZhangBao-YanB... | lld:pubmed |
| pubmed-article:17892535 | pubmed:author | pubmed-author:RestrepoRicar... | lld:pubmed |
| pubmed-article:17892535 | pubmed:author | pubmed-author:NothwehrSteve... | lld:pubmed |
| pubmed-article:17892535 | pubmed:author | pubmed-author:PeterHaraldH | lld:pubmed |
| pubmed-article:17892535 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17892535 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:17892535 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17892535 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17892535 | pubmed:pagination | 1841-53 | lld:pubmed |
| pubmed-article:17892535 | pubmed:dateRevised | 2011-1-27 | lld:pubmed |
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| pubmed-article:17892535 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17892535 | pubmed:articleTitle | Structural features of vps35p involved in interaction with other subunits of the retromer complex. | lld:pubmed |
| pubmed-article:17892535 | pubmed:affiliation | Division of Biological Sciences, 401 Tucker Hall, University of Missouri, Columbia, MO 65211, USA. | lld:pubmed |
| pubmed-article:17892535 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17892535 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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