biostudies-literatureRybakin VNIAID NIH HHSNHLBI NIH HHSNIGMS NIH HHS1251-6https://www.ebi.ac.uk/biostudies/studies/S-EPMC3245696biostudies-literatureUnknown12(12)Bimolecular fluorescence complementation was used to engineer CD8 molecules so that CD8?? and CD8?? dimers can be independently visualized on the surface of a T cell during antigen recognition. Using this approach, we show that CD8?? is recruited to the immunological synapse almost as well as CD8??, but because the kinase Lck associates preferentially with CD8?? in lipid rafts, CD8?? is the weaker co-receptor. During recognition of the strong CD8?? ligand H2-TL, CD8?? is preferentially recruited. Thus, recruitment of the two CD8 species correlates with their relative binding to the available ligands, rather than with the co-receptor functions of the CD8 species.EMBO reportsCD8?? and -?? isotypes are equally recruited to the immunological synapse through their ability to bind to MHC class I.PMC3245696R01AI074074R01 GM065230T32 HL007195R01GM065230R01 AI074074T32HL07195Ampudia JRybakin VClamme JPYachi PPGascoigne NRfalseCD8?? and -?? isotypes are equally recruited to the immunological synapse through their ability to bind to MHC class I.Bimolecular fluorescence complementation was used to engineer CD8 molecules so that CD8?? and CD8?? dimers can be independently visualized on the surface of a T cell during antigen recognition. Using this approach, we show that CD8?? is recruited to the immunological synapse almost as well as CD8??, but because the kinase Lck associates preferentially with CD8?? in lipid rafts, CD8?? is the weaker co-receptor. During recognition of the strong CD8?? ligand H2-TL, CD8?? is preferentially recruited. Thus, recruitment of the two CD8 species correlates with their relative binding to the available ligands, rather than with the co-receptor functions of the CD8 species.2011-01-01T00:00:00Z2011 Dec2021-03-07T08:39:03Z2019-03-27T00:47:21ZS-EPMC32456962208114410.1038/embor.2011.209