pubmed-article:20713601 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20713601 | lifeskim:mentions | umls-concept:C0221102 | lld:lifeskim |
pubmed-article:20713601 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
pubmed-article:20713601 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
pubmed-article:20713601 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:20713601 | pubmed:dateCreated | 2010-8-24 | lld:pubmed |
pubmed-article:20713601 | pubmed:abstractText | BAG-6/Scythe/BAT3 is a ubiquitin-like protein that was originally reported to be the product of a novel gene located within the human major histocompatibility complex, although the mechanisms of its function remain largely obscure. Here, we demonstrate the involvement of BAG-6 in the degradation of a CL1 model defective protein substrate in mammalian cells. We show that BAG-6 is essential for not only model substrate degradation but also the ubiquitin-mediated metabolism of newly synthesized defective polypeptides. Furthermore, our in vivo and in vitro analysis shows that BAG-6 interacts physically with puromycin-labeled nascent chain polypeptides and regulates their proteasome-mediated degradation. Finally, we show that knockdown of BAG-6 results in the suppressed presentation of MHC class I on the cell surface, a procedure known to be affected by the efficiency of metabolism of defective ribosomal products. Therefore, we propose that BAG-6 is necessary for ubiquitin-mediated degradation of newly synthesized defective polypeptides. | lld:pubmed |
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pubmed-article:20713601 | pubmed:language | eng | lld:pubmed |
pubmed-article:20713601 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20713601 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20713601 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20713601 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:20713601 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:20713601 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:20713601 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20713601 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20713601 | pubmed:month | Aug | lld:pubmed |
pubmed-article:20713601 | pubmed:issn | 1540-8140 | lld:pubmed |
pubmed-article:20713601 | pubmed:author | pubmed-author:YokosawaHidey... | lld:pubmed |
pubmed-article:20713601 | pubmed:author | pubmed-author:KawaharaHiroy... | lld:pubmed |
pubmed-article:20713601 | pubmed:author | pubmed-author:MinamiRyosuke... | lld:pubmed |
pubmed-article:20713601 | pubmed:author | pubmed-author:KagawaHirokiH | lld:pubmed |
pubmed-article:20713601 | pubmed:author | pubmed-author:HayakawaAtsuk... | lld:pubmed |
pubmed-article:20713601 | pubmed:author | pubmed-author:YanagiYukoY | lld:pubmed |
pubmed-article:20713601 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20713601 | pubmed:day | 23 | lld:pubmed |
pubmed-article:20713601 | pubmed:volume | 190 | lld:pubmed |
pubmed-article:20713601 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20713601 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20713601 | pubmed:pagination | 637-50 | lld:pubmed |
pubmed-article:20713601 | pubmed:dateRevised | 2011-9-28 | lld:pubmed |
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