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pubmed-article:20713601pubmed:dateCreated2010-8-24lld:pubmed
pubmed-article:20713601pubmed:abstractTextBAG-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:20713601pubmed:authorpubmed-author:YokosawaHidey...lld:pubmed
pubmed-article:20713601pubmed:authorpubmed-author:KawaharaHiroy...lld:pubmed
pubmed-article:20713601pubmed:authorpubmed-author:MinamiRyosuke...lld:pubmed
pubmed-article:20713601pubmed:authorpubmed-author:KagawaHirokiHlld:pubmed
pubmed-article:20713601pubmed:authorpubmed-author:HayakawaAtsuk...lld:pubmed
pubmed-article:20713601pubmed:authorpubmed-author:YanagiYukoYlld:pubmed
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pubmed-article:20713601pubmed:pagination637-50lld:pubmed
pubmed-article:20713601pubmed:dateRevised2011-9-28lld:pubmed
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