title: Assembly and function of the major histocompatibility complex (MHC) I peptide-loading complex are conserved across higher vertebrates.
abstract: 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.
authors.affiliation: From the Institute of Biochemistry, Biocenter and.
authors.forename: Andreas
authors.initials: A
authors.lastname: Hinz
authors.affiliation: From the Institute of Biochemistry, Biocenter and.
authors.forename: Johanna
authors.initials: J
authors.lastname: Jedamzick
authors.affiliation: From the Institute of Biochemistry, Biocenter and.
authors.forename: Valentina
authors.initials: V
authors.lastname: Herbring
authors.affiliation: From the Institute of Biochemistry, Biocenter and.
authors.forename: Hanna
authors.initials: H
authors.lastname: Fischbach
authors.affiliation: Georg-Speyer-Haus, Institute for Tumor Biology and Experimental Therapy, Paul-Ehrlich-Str. 42, 60596 Frankfurt/M., Germany.
authors.forename: Jessica
authors.initials: J
authors.lastname: Hartmann
authors.affiliation: From the Institute of Biochemistry, Biocenter and.
authors.forename: David
authors.initials: D
authors.lastname: Parcej
authors.affiliation: Georg-Speyer-Haus, Institute for Tumor Biology and Experimental Therapy, Paul-Ehrlich-Str. 42, 60596 Frankfurt/M., Germany.
authors.forename: Joachim
authors.initials: J
authors.lastname: Koch
authors.affiliation: From the Institute of Biochemistry, Biocenter and Cluster of Excellence-Macromolecular Complexes, Goethe-University, Max-von-Laue-Str. 9, 60438 Frankfurt/M., Germany and tampe@em.uni-frankfurt.de.
authors.forename: Robert
authors.initials: R
authors.lastname: Tampé
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D001717:Birds; D002417:Cattle; D004285:Dogs; D019143:Evolution, Molecular; D015395:Histocompatibility Antigens Class I / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D006801:Humans; D026901:Membrane Transport Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D051379:Mice; D046912:Multiprotein Complexes / Q000276:immunology / Q000378:metabolism; D055503:Protein Multimerization / Q000502:physiology; D051381:Rats; D013045:Species Specificity; D034421:Sus scrofa
chemical_list: D018528:ATP-Binding Cassette Transporters; D015395:Histocompatibility Antigens Class I; D026901:Membrane Transport Proteins; D046912:Multiprotein Complexes; C107762:tapasin
keywords: ABC Transporter; Antigen Processing; Immunology; Major Histocompatibility Complex (MHC); Membrane Protein; Transporter