TY - JOUR A1 - Hinz, Andreas A1 - Jedamzick, Johanna A1 - Herbring, Valentina A1 - Fischbach, Hanna A1 - Hartmann, Jessica A1 - Parcej, David A1 - Koch, Joachim A1 - Tampé, Robert T1 - Assembly and function of the major histocompatibility complex (MHC) I peptide-loading complex are conserved across higher vertebrates T2 - Journal of biological chemistry N2 - Antigen presentation to cytotoxic T lymphocytes via major histocompatibility complex class I (MHC I) molecules depends on the heterodimeric transporter associated with antigen processing (TAP). For efficient antigen supply to MHC I molecules in the ER, TAP assembles a macromolecular peptide-loading complex (PLC) by recruiting tapasin. In evolution, TAP appeared together with effector cells of adaptive immunity at the transition from jawless to jawed vertebrates and diversified further within the jawed vertebrates. Here, we compared TAP function and interaction with tapasin of a range of species within two classes of jawed vertebrates. We found that avian and mammalian TAP1 and TAP2 form heterodimeric complexes across taxa. Moreover, the extra N-terminal domain TMD0 of mammalian TAP1 and TAP2 as well as avian TAP2 recruits tapasin. Strikingly, however, only TAP1 and TAP2 from the same taxon can form a functional heterodimeric translocation complex. These data demonstrate that the dimerization interface between TAP1 and TAP2 and the tapasin docking sites for PLC assembly are conserved in evolution, whereas elements of antigen translocation diverged later in evolution and are thus taxon specific. KW - ABC Transporter KW - Antigen Processing KW - Immunology KW - Major Histocompatibility Complex (MHC) KW - Membrane Protein KW - Transporter Y1 - 2021 UR - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/76989 UR - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-769897 SN - 0021-9258 VL - 289.2014 IS - 48 SP - 33109 EP - 33117 PB - American Society for Biochemistry and Molecular Biology Publications CY - Bethesda, Md ER -