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Retention of empty MHC class I molecules by tapasin is essential to reconstitute antigen presentation in invertebrate cells
Author(s) -
Schoenhals Gary J.,
Krishna R.Murli,
Grandea Andres G.,
Spies Thomas,
Peterson Per A.,
Yang Young,
Früh Klaus
Publication year - 1999
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/18.3.743
Subject(s) - biology , mhc class i , antigen processing , antigen presentation , transporter associated with antigen processing , major histocompatibility complex , antigen , microbiology and biotechnology , cross presentation , genetics , t cell , immune system
Presentation of antigen‐derived peptides by major histocompatibility complex (MHC) class I molecules is dependent on an endoplasmic reticulum (ER) resident glycoprotein, tapasin, which mediates their interaction with the transporter associated with antigen processing (TAP). Independently of TAP, tapasin was required for the presentation of peptides targeted to the ER by signal sequences in MHC class I‐transfected insect cells. Tapasin increased MHC class I peptide loading by retaining empty but not peptide‐containing MHC class I molecules in the ER. Upon co‐expression of TAP, this retention/release function of tapasin was sufficient to reconstitute MHC class I antigen presentation in insect cells, thus defining the minimal non‐housekeeping functions required for MHC class I antigen presentation.