Interleukin (IL-)11 is involved in various processes including regeneration, and embryo implantation. IL-11 signaling via individual IL-11a-receptor splice variants IL-11R1 or IL-11R2 and gp130 is frequently conducted at cellular barriers. Here we show that biologically active IL-11R1/2:gp130 receptor complexes localize on apical and basolateral membranes of polarized cells, whereas IL-6 signaling via IL-6R:gp130 complexes is restricted to the basolateral side. Consequently, IL-11R1/2 forces apical redirection of gp130. Moreover, basolaterally supplied IL-11 is transported and released to the apical extracellular space via transcytosis and exclusively mediated by IL-11R1, whereas the IL-6R and IL-11R2 has no transcytosis activity. In addition, we show that transcytosis of IL-11 is dependent on the intracellular domain of IL-11R1, and synthetic transfer of the intracellular domain of IL-11R1 to IL-6R facilitates transcytosis of IL-6. Our data define IL-11R as a cytokine receptor with transcytotic activity by which IL-11 and IL-6:soluble IL-6R complexes are transported across cellular barriers.