Introduction: Interleukin-11 (IL-11) is a pleiotropic cytokine with wide biological activities in bone and hematologic compartments. Its activity is mediated by binding to a multisubunit complex formed by the IL-11-specific receptor α-chain (IL-11Rα) and the signal-transducing receptor β-chain (gp130). Controlled expression of IL-11Rα is therefore a key element regulating IL-11 binding and responsiveness. In this study we describe how, in the course of identifying human IL-11Rα gene transcriptional start sites, we found a transcript corresponding to a fusion protein between galactose-1-phosphate uridyl transferase (GALT) and IL-11Rα.Materials and Methods: Expression analysis of the fusion transcript was performed using RT-PCR, RNase protection, genomic cloning. Functionality of the fusion protein was investigated by IL-11 receptor complex reconstitution in BA/F3 cells and by measuring GALT activity in cellular extracts of transfected COS cells.Results: GALT and IL-11Rα genes loci on chromosome 9p13 are spaced by only 4 kb. The intergenic fusion transcript does not contain the last exon of GALT gene as well as the putative exon 1 of IL-11Rα gene, the resulting mRNA codes for a fusion protein associating GALT and IL11Rα. This mRNA is present at low levels in human cells. The fusion protein is targeted to plasma membrane and does not appear to be functional as ligand-specific receptor α-chain or as transferase enzyme.Conclusion: The level of the GALT-IL-11Rα fusion mRNA is low when compared to the level of the GALT mRNA, but very important when compared to that of the IL11Rα mRNA. These results suggest that the fusion product could antagonize and/or regulate formation of functional IL-11 receptor complexes.