| pubmed-article:21184741 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21184741 | lifeskim:mentions | umls-concept:C1332002 | lld:lifeskim |
| pubmed-article:21184741 | lifeskim:mentions | umls-concept:C0205160 | lld:lifeskim |
| pubmed-article:21184741 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:21184741 | lifeskim:mentions | umls-concept:C1539270 | lld:lifeskim |
| pubmed-article:21184741 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:21184741 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:21184741 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:21184741 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:21184741 | pubmed:dateCreated | 2011-1-24 | lld:pubmed |
| pubmed-article:21184741 | pubmed:abstractText | Human breast cancer resistance protein (BCRP)/MXR/ABCG2 is a well-recognized ABC half-transporter that is highly expressed at the apical membrane of many normal tissues and cancer cells. BCRP facilitates disposition of endogenous and exogenous harmful xenobiotics to protect cells/tissues from xenobiotic-induced toxicity. Despite the enormous impact of BCRP in the physiological and pathophysiological regulation of the transport of a wide variety of substrates, little is known about the factors that regulate posttranslational expression of BCRP. Here, we identified Derlin-1, a member of a family of proteins that bears homology to yeast Der1p, as a posttranslational regulator of BCRP expression. Overexpression of Derlin-1 suppressed ER to Golgi transport of wild-type (WT) BCRP that is known to be efficiently trafficked to the plasma membrane. On the other hand, protein expression of N596Q variant of BCRP, N-linked glycosylation-deficient mutant that preferentially undergoes ubiquitin-mediated ER-associated degradation (ERAD), was strongly suppressed by the overexpression of Derlin-1, whereas knockdown of Derlin-1 stabilized N596Q protein, suggesting a negative regulatory role of Derlin-1 for N596Q protein expression. Notably, knockdown of Derlin-1 also stabilized the expression of tunicamycin-induced deglycosylated WT BCRP protein, implying the importance of glycosylation state for the recognition of BCRP by Derlin-1. Thus, our data demonstrate that Derlin-1 is a negative regulator for both glycosylated and non-glycosylated BCRP expression and provide a novel posttranslational regulatory mechanism of BCRP by Derlin-1. | lld:pubmed |
| pubmed-article:21184741 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21184741 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21184741 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21184741 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21184741 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21184741 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21184741 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21184741 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21184741 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21184741 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:21184741 | pubmed:issn | 1090-2104 | lld:pubmed |
| pubmed-article:21184741 | pubmed:author | pubmed-author:SatoTakashiT | lld:pubmed |
| pubmed-article:21184741 | pubmed:author | pubmed-author:SugiyamaYuich... | lld:pubmed |
| pubmed-article:21184741 | pubmed:author | pubmed-author:KusuharaHiroy... | lld:pubmed |
| pubmed-article:21184741 | pubmed:author | pubmed-author:ShutoTsuyoshi... | lld:pubmed |
| pubmed-article:21184741 | pubmed:author | pubmed-author:KaiHirofumiH | lld:pubmed |
| pubmed-article:21184741 | pubmed:author | pubmed-author:CyrDouglas... | lld:pubmed |
| pubmed-article:21184741 | pubmed:author | pubmed-author:SuzukiShingoS | lld:pubmed |
| pubmed-article:21184741 | pubmed:author | pubmed-author:SuicoMary... | lld:pubmed |
| pubmed-article:21184741 | pubmed:author | pubmed-author:SugiyamaTakas... | lld:pubmed |
| pubmed-article:21184741 | pubmed:author | pubmed-author:KogaTomoakiT | lld:pubmed |
| pubmed-article:21184741 | pubmed:copyrightInfo | Copyright © 2010 Elsevier Inc. All rights reserved. | lld:pubmed |
| pubmed-article:21184741 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21184741 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:21184741 | pubmed:volume | 404 | lld:pubmed |
| pubmed-article:21184741 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21184741 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21184741 | pubmed:pagination | 853-8 | lld:pubmed |
| pubmed-article:21184741 | pubmed:meshHeading | pubmed-meshheading:21184741... | lld:pubmed |
| pubmed-article:21184741 | pubmed:meshHeading | pubmed-meshheading:21184741... | lld:pubmed |
| pubmed-article:21184741 | pubmed:meshHeading | pubmed-meshheading:21184741... | lld:pubmed |
| pubmed-article:21184741 | pubmed:meshHeading | pubmed-meshheading:21184741... | lld:pubmed |
| pubmed-article:21184741 | pubmed:meshHeading | pubmed-meshheading:21184741... | lld:pubmed |
| pubmed-article:21184741 | pubmed:meshHeading | pubmed-meshheading:21184741... | lld:pubmed |
| pubmed-article:21184741 | pubmed:meshHeading | pubmed-meshheading:21184741... | lld:pubmed |
| pubmed-article:21184741 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21184741 | pubmed:articleTitle | Posttranslational negative regulation of glycosylated and non-glycosylated BCRP expression by Derlin-1. | lld:pubmed |
| pubmed-article:21184741 | pubmed:affiliation | Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Global COE Cell Fate Regulation Research and Education Unit, Kumamoto University, 5-1 Oe-Honmachi, Kumamoto 862-0973, Japan. | lld:pubmed |
| pubmed-article:21184741 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21184741 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:9429 | entrezgene:pubmed | pubmed-article:21184741 | lld:entrezgene |
| entrez-gene:79139 | entrezgene:pubmed | pubmed-article:21184741 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21184741 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21184741 | lld:entrezgene |
