| pubmed-article:15187134 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15187134 | lifeskim:mentions | umls-concept:C0019629 | lld:lifeskim |
| pubmed-article:15187134 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
| pubmed-article:15187134 | lifeskim:mentions | umls-concept:C1428347 | lld:lifeskim |
| pubmed-article:15187134 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:15187134 | pubmed:dateCreated | 2004-6-9 | lld:pubmed |
| pubmed-article:15187134 | pubmed:abstractText | In this study, we examine the role of the putative cargo receptor B cell-associated protein (Bap)29/31 in the export of MHC class I molecules out of the endoplasmic reticulum (ER). We show that Bap31 binds to two allotypes of mouse class I molecules, with the interaction initiated at the time of H chain association with beta(2)-microglobulin and maintained until the class I molecule has left the ER. We also show that Bap31 is part of the peptide-loading complex, although is not required for its formation. Bap31 binds not only to class I molecules, but can bind to tapasin in the absence of class I. Consistent with an important role in recruiting class I molecules to transport vesicles, we show that in the absence of Bap29/31, there is a loss of class I colocalization with mSec31 (p137), a component of mammalian coat protein complex II coats. This observation is also associated with a delay in class I traffic from ER to Golgi. Our results are consistent with the view that class I molecules are largely recruited to ER exit sites by Bap29/31, and that Bap29/31 is a cargo receptor for MHC class I molecules. | lld:pubmed |
| pubmed-article:15187134 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15187134 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15187134 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:15187134 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15187134 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:15187134 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:15187134 | pubmed:author | pubmed-author:ShoreGordon... | lld:pubmed |
| pubmed-article:15187134 | pubmed:author | pubmed-author:PaquetMarie-E... | lld:pubmed |
| pubmed-article:15187134 | pubmed:author | pubmed-author:WilliamsDavid... | lld:pubmed |
| pubmed-article:15187134 | pubmed:author | pubmed-author:Cohen-DoyleMy... | lld:pubmed |
| pubmed-article:15187134 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15187134 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15187134 | pubmed:volume | 172 | lld:pubmed |
| pubmed-article:15187134 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15187134 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15187134 | pubmed:pagination | 7548-55 | lld:pubmed |
| pubmed-article:15187134 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15187134 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15187134 | pubmed:articleTitle | Bap29/31 influences the intracellular traffic of MHC class I molecules. | lld:pubmed |
| pubmed-article:15187134 | pubmed:affiliation | Department of Immunology, University of Toronto, Toronto, Ontario M5S 1A8, Canada. | lld:pubmed |
| pubmed-article:15187134 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15187134 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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