rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1999-10-1
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pubmed:abstractText |
Recent studies demonstrate that processing of N-linked glycans plays an important role in the quality control of major histocompatibility complex (MHC) class I transport from the endoplasmic reticulum (ER) to the Golgi complex and beyond. Here, we investigated the importance of oligosaccharide chain length on the association of MHC class I proteins with molecular chaperones and their intracellular transport from the ER to the Golgi. These data show that calnexin interaction with class I proteins having truncated N-glycans was reduced compared to normal class I molecules, whereas the assembly of class I with calreticulin and TAP was unperturbed by N-glycan chain length. Additionally, these results demonstrate that class I proteins containing truncated N-glycans showed decreased detachment from calreticulin and TAP relative to class I proteins bearing typical oligosaccharides. Taken together, these studies show that N-glycan chain length is an important determinant for the quality control of newly synthesized MHC class I proteins in the ER.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calnexin,
http://linkedlifedata.com/resource/pubmed/chemical/Calreticulin,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/H-2 Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/H-2Kb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/beta 2-Microglobulin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author |
|
pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
473-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10462499-ATP-Binding Cassette Transporters,
pubmed-meshheading:10462499-Animals,
pubmed-meshheading:10462499-Biological Transport,
pubmed-meshheading:10462499-Calcium-Binding Proteins,
pubmed-meshheading:10462499-Calnexin,
pubmed-meshheading:10462499-Calreticulin,
pubmed-meshheading:10462499-Carbohydrate Sequence,
pubmed-meshheading:10462499-Endoplasmic Reticulum,
pubmed-meshheading:10462499-Glycoproteins,
pubmed-meshheading:10462499-Golgi Apparatus,
pubmed-meshheading:10462499-H-2 Antigens,
pubmed-meshheading:10462499-Mice,
pubmed-meshheading:10462499-Molecular Chaperones,
pubmed-meshheading:10462499-Molecular Sequence Data,
pubmed-meshheading:10462499-Protein Binding,
pubmed-meshheading:10462499-Ribonucleoproteins,
pubmed-meshheading:10462499-beta 2-Microglobulin
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pubmed:year |
1999
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pubmed:articleTitle |
Influence of N-glycan chain length on chaperone association and intracellular transport of major histocompatibility complex class I proteins.
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pubmed:affiliation |
School of Medicine, East Carolina University, Greenville, North Carolina, 27858-4354, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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