Transforming growth factor β (TGF-β) signaling involves interactions of at least two different receptors, types I (TβRI) and II (TβRII), which form ligand-mediated heteromeric complexes. Although we have shown in the past that TβRII in the absence of ligand is a homodimer on the cell surface, TβRI has not been similarly investigated, and the site of complex formation is not known for either receptor. Several studies have indicated that homomeric interactions are involved in TGF-β signaling and regulation, emphasizing the importance of a detailed understanding of the homooligomerization of TβRI or TβRII. Here we have combined complementary approaches to study these homomeric interactions in both naturally expressing cell lines and cells cotransfected with various combinations of epitope-tagged type I or type II receptors. We used sedimentation velocity of metabolically labeled receptors on sucrose gradients to show that both TβRI and TβRII form homodimer-sized complexes in the endoplasmic reticulum, and we used coimmunoprecipitation studies to demonstrate the existence of type I homooligomers. Using a technique based on antibody-mediated immunofluorescence copatching of receptors carrying different epitope tags, we have demonstrated ligand-independent homodimers of TβRI on the surface of live cells. Soluble forms of both receptors are secreted as monomers, indicating that the ectodomains are not sufficient to mediate homodimerization, although TGF-β1 is able to promote dimerization of the type II receptor ectodomain. These findings may have important implications for the regulation of TGF-β signaling.