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Cell Res. 2010 Nov;20(11):1216-23. doi: 10.1038/cr.2010.105. Epub 2010 Jul 13.

Monomeric type I and type III transforming growth factor-β receptors and their dimerization revealed by single-molecule imaging.

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Beijing National Laboratory for Molecular Sciences, Institute of Chemistry, Key Laboratory of Molecular Nanostructures and Nanotechnology, Chinese Academy of Sciences, Beijing 100190, China.


Transforming growth factor-β (TGF-β) binds with two transmembrane serine/threonine kinase receptors, type II (TβRII) and type I receptors (TβRI), and one accessory receptor, type III receptor (TβRIII), to transduce signals across cell membranes. Previous biochemical studies suggested that TβRI and TβRIII are preexisted homo-dimers. Using single-molecule microscopy to image green fluorescent protein-labeled membrane proteins, for the first time we have demonstrated that TβRI and TβRIII could exist as monomers at a low expression level. Upon TGF-β1 stimulation, TβRI follows the general ligand-induced receptor dimerization model for activation, but this process is TβRII-dependent. The monomeric status of the non-kinase receptor TβRIII is unchanged in the presence of TGF-β1. With the increase of receptor expression, both TβRI and TβRIII can be assembled into dimers on cell surfaces.

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