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题名: Single-Molecule Imaging Reveals the Activation Dynamics of Intracellular Protein Smad3 on Cell Membrane
作者: Li, Nan1, 2; Yang, Yong1; He, Kangmin1; Zhang, Fayun3; Zhao, Libo1; Zhou, Wei1, 2; Yuan, Jinghe1; Liang, Wei3; Fang, Xiaohong1, 2
刊名: SCIENTIFIC REPORTS
发表日期: 2016-09-19
卷: 6
收录类别: SCI
英文摘要: Smad3 is an intracellular protein that plays a key role in propagating transforming growth factor beta (TGF-beta) signals from cell membrane to nucleus. However whether the transient process of Smad3 activation occurs on cell membrane and how it is regulated remains elusive. Using advanced live-cell single-molecule fluorescence microscopy to image and track fluorescent protein-labeled Smad3, we observed and quantified, for the first time, the dynamics of individual Smad3 molecules docking to and activation on the cell membrane. It was found that Smad3 docked to cell membrane in both unstimulated and stimulated cells, but with different diffusion rates and dissociation kinetics. The change in its membrane docking dynamics can be used to study the activation of Smad3. Our results reveal that Smad3 binds with type I TGF-beta receptor (TRI) even in unstimulated cells. Its activation is regulated by TRI phosphorylation but independent of receptor endocytosis. This study offers new information on TGF-beta/Smad signaling, as well as a new approach to investigate the activation of intracellular signaling proteins for a better understanding of their functions in signal transduction.
语种: 英语
内容类型: 期刊论文
URI标识: http://ir.iccas.ac.cn/handle/121111/35259
Appears in Collections:分子纳米结构与纳米技术实验室_期刊论文

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作者单位: 1.Chinese Acad Sci, Inst Chem, Beijing Natl Lab Mol Sci, Key Lab Mol Nanostruct & Nanotechnol, Beijing 100190, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Chinese Acad Sci, Inst Biophys, Key Lab Prot & Peptide Drugs, Beijing 100101, Peoples R China
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