The transporter associated with antigen processing (TAP) delivers cyto
solic peptides into the endoplasmic reticulum (ER) where they bind to
nascent class I histocompatibility molecules. Class I-peptide complexe
s are then displayed at the cell surface for recognition by cytotoxic
T lymphocytes. Immunoprecipitation of either TAP or class I molecules
revealed an association between the transporter and diverse class I pr
oducts. TAP bound preferentially to heterodimers of the class I heavy
chain and beta(2)-microglobulin, and the complex subsequently dissocia
ted in parallel with transport of class I molecules from the ER to the
Golgi apparatus. The TAP-class I complexes could also be dissociated
in vitro by the addition of class I-binding peptides. The association
of class I molecules with TAP likely promotes efficient capture of pep
tides before their exposure to the lumen of the ER.