Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1998-8-5
|
pubmed:abstractText |
Classical class I molecules assemble in the endoplasmic reticulum (ER) with peptides mostly generated from cytosolic proteins by the proteasome. The activity of the proteasome can be modulated by a variety of accessory protein complexes. A subset of the proteasome beta-subunits (LMP2, LMP7, and MECL-1) and one of the accessory complexes, PA28, are upregulated by gamma-interferon and affect the generation of peptides to promote more efficient antigen recognition. The peptides are translocated into the ER by the transporter associated with antigen processing (TAP). A transient complex containing a class I heavy chain-beta 2 microglobulin (beta 2 m) dimer is assembled onto the TAP molecule by successive interactions with the ER chaperones calnexin and calreticulin and a specialized molecule, tapasin. Peptide binding releases the class I-beta 2 m dimer for transport to the cell surface, while lack of binding results in proteasome-mediated degradation. The products of certain nonclassical MHC-linked class I genes bind peptides in a similar way. A homologous set of beta 2 m-associated membrane glycoproteins, the CD1 molecules, appears to bind lipid-based ligands within the endocytic pathway.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class I,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/beta 2-Microglobulin
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0732-0582
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
16
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
323-58
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:9597133-ATP-Binding Cassette Transporters,
pubmed-meshheading:9597133-Animals,
pubmed-meshheading:9597133-Antigen Presentation,
pubmed-meshheading:9597133-Cysteine Endopeptidases,
pubmed-meshheading:9597133-Dimerization,
pubmed-meshheading:9597133-Endoplasmic Reticulum,
pubmed-meshheading:9597133-Histocompatibility Antigens Class I,
pubmed-meshheading:9597133-Humans,
pubmed-meshheading:9597133-Multienzyme Complexes,
pubmed-meshheading:9597133-Proteasome Endopeptidase Complex,
pubmed-meshheading:9597133-beta 2-Microglobulin
|
pubmed:year |
1998
|
pubmed:articleTitle |
Mechanisms of MHC class I--restricted antigen processing.
|
pubmed:affiliation |
Department of Internal Medicine and Section of Immunobiology, Yale University School of Medicine, Howard Hughes Medical Institute, New Haven, CT 06510, USA. eric.pamer@yale.edu
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
|