Henis Y I, Moustakas A, Lin H Y, Lodish H F
Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142.
J Cell Biol. 1994 Jul;126(1):139-54. doi: 10.1083/jcb.126.1.139.
Affinity-labeling experiments have detected hetero-oligomers of the types I, II, and III transforming growth factor beta (TGF-beta) receptors which mediate intracellular signaling by TGF-beta, but the oligomeric state of the individual receptor types remains unknown. Here we use two types of experiments to show that a major portion of the receptor types II and III forms homo-oligomers both in the absence and presence of TGF-beta. Both experiments used COS-7 cells co-transfected with combinations of these receptors carrying different epitope tags at their extracellular termini. In immunoprecipitation experiments, radiolabeled TGF-beta was bound and cross-linked to cells co-expressing two differently tagged type II receptors. Sequential immunoprecipitations using anti-epitope monoclonal antibodies showed that type II TGF-beta receptors form homo-oligomers. In cells co-expressing epitope-tagged types II and III receptors, a low level of co-precipitation of the ligand-labeled receptors was observed, indicating that some hetero-oligomers of the types II and III receptors exist in the presence of ligand. Antibody-mediated cross-linking studies based on double-labeling immunofluorescence explored co-patching of the receptors at the cell surface on live cells. In cells co-expressing two differently tagged type II receptors or two differently tagged type III receptors, forcing one receptor into micropatches by IgG induced co-patching of the receptor carrying the other tag, labeled by noncross-linking monovalent Fab'. These studies showed that homo-oligomers of the types II and III receptors exist on the cell surface in the absence or presence of TGF-beta 1 or -beta 2. In cells co-expressing types II and III receptors, the amount of heterocomplexes at the cell surface was too low to be detected in the immunofluorescence co-patching experiments, confirming that hetero-oligomers of the types II and III receptors are minor and probably transient species.
亲和标记实验已检测到I、II和III型转化生长因子β(TGF-β)受体的异源寡聚体,这些受体介导TGF-β的细胞内信号传导,但各个受体类型的寡聚状态仍不清楚。在此,我们使用两种类型的实验来表明,在不存在和存在TGF-β的情况下,II型和III型受体的主要部分均形成同源寡聚体。这两种实验均使用了在细胞外末端携带不同表位标签的这些受体组合共转染的COS-7细胞。在免疫沉淀实验中,放射性标记的TGF-β与共表达两种不同标记的II型受体的细胞结合并交联。使用抗表位单克隆抗体进行的连续免疫沉淀表明,II型TGF-β受体形成同源寡聚体。在共表达表位标记的II型和III型受体的细胞中,观察到配体标记的受体有低水平的共沉淀,表明在配体存在的情况下存在一些II型和III型受体的异源寡聚体。基于双标记免疫荧光的抗体介导交联研究探索了活细胞表面受体的共斑块形成。在共表达两种不同标记的II型受体或两种不同标记的III型受体的细胞中,通过IgG将一种受体强制形成微斑块会诱导携带另一种标签的受体共斑块形成,该受体由非交联单价Fab'标记。这些研究表明,在不存在或存在TGF-β1或-β2的情况下,II型和III型受体的同源寡聚体存在于细胞表面。在共表达II型和III型受体的细胞中,细胞表面异源复合物的量太低,无法在免疫荧光共斑块形成实验中检测到,这证实了II型和III型受体的异源寡聚体是次要的且可能是瞬时存在的物种。