Tapasin: an ER chaperone that controls MHC class I assembly with peptide.

Grandea AG, Van Kaer L
Trends Immunol. 2001 22 (4): 194-9

PMID: 11274924 · DOI:10.1016/s1471-4906(01)01861-0

The stable assembly of MHC class I molecules with peptides in the endoplasmic reticulum (ER) involves several accessory molecules. One of these accessory molecules is tapasin, a transmembrane protein that tethers empty class I molecules to the peptide transporter associated with antigen processing (TAP). Here, evidence is presented that tapasin retains class I molecules in the ER until they acquire high-affinity peptides.

MeSH Terms (13)

Animals Antigen Presentation Antiporters ATP-Binding Cassette Transporters ATP Binding Cassette Transporter, Subfamily B, Member 2 ATP Binding Cassette Transporter, Subfamily B, Member 3 Endoplasmic Reticulum Histocompatibility Antigens Class I Humans Immunoglobulins Membrane Transport Proteins Molecular Chaperones Peptides

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