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When incubated with [³H]myristate or [³H]palmitate, LSTRA cells, a murine T cell line, incorporated radiolabel into a protein of 95 kDa as analyzed by SDS-polyacrylamide gel electrophoresis. This dually acylated protein was identified as the transferrin receptor by immunoprecipitation with a monoclonal anti-transferrin receptor antibody. Acylation of the transferrin receptor was posttranslational and occurred via ester or thioester linkages. Analysis of radiolabeled transferrin receptor protein^a from [³H]myristate-labeled cells by acid hydrolysis followed by thin layer chromatography revealed the exclusive presence of [³H]myristate. Labeled transferrin receptor protein from [³H]palmitate-labeled cells contained predominantly [³H]stearate and smaller amounts of [³H]palmitate. This is in contrast to the protein-tyrosine kinase p56^lck, which in [³H]palmitate-treated LSTRA cells, incorporated primarily [³H]palmitate. An …