Impaired assembly yet normal trafficking of MHC class I molecules in Tapasin mutant mice.

Grandea AG, Golovina TN, Hamilton SE, Sriram V, Spies T, Brutkiewicz RR, Harty JT, Eisenlohr LC, Van Kaer L
Immunity. 2000 13 (2): 213-22

PMID: 10981964 · DOI:10.1016/s1074-7613(00)00021-2

Loading of peptides onto major histocompatibility complex class I molecules involves a multifactorial complex that includes tapasin (TPN), a membrane protein that tethers empty class I glycoproteins to the transporter associated with antigen processing. To evaluate the in vivo role of TPN, we have generated Tpn mutant mice. In these animals, most class I molecules exit the endoplasmic reticulum (ER) in the absence of stably bound peptides. Consequently, mutant animals have defects in class I cell surface expression, antigen presentation, CD8+ T cell development, and immune responses. These findings reveal a critical role of TPN for ER retention of empty class I molecules. Tpn mutant animals should prove useful for studies on alternative antigen-processing pathways that involve post-ER peptide loading.

MeSH Terms (10)

Animals Antigen Presentation Antiporters Biological Transport Gene Expression Regulation Histocompatibility Antigens Class I Immunoglobulins Membrane Transport Proteins Mice Mutation

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