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Fluorescence Biomembrane Force Probe: Concurrent Quantitation of Receptor-ligand Kinetics and Binding-induced Intracellular Signaling on a Single Cell
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Single-molecule force spectroscopy study of interaction between transforming growth factor beta1 and its receptor in

Junping Yu1, Qiang Wang, Xiaoli Shi

  • 1Beijing National Laboratory for Molecular Sciences, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, People's Republic of China.

The Journal of Physical Chemistry. B
|November 14, 2007
PubMed

Insights

Transforming growth factor beta1 (TGF-beta1) binding to its receptors is crucial for cell signaling. This study reveals that TGF-beta1 binds more stably to the receptor complex after type I receptor recruitment, clarifying signaling mechanisms.

Area of Science:

  • Cell Biology
  • Biophysics
  • Molecular Signaling

Background:

  • Transforming growth factor beta1 (TGF-beta1) is a key regulator of cellular processes.
  • TGF-beta1 signaling initiates via interactions with TGF-beta type II receptor (TbetaRII) and type I receptor (TbetaRI).
  • The precise molecular mechanism of TGF-beta1 ligand-receptor complex formation in living cells remains incompletely understood.

Purpose of the Study:

  • To investigate the interaction dynamics between TGF-beta1 and its receptors in living cells using single-molecule force spectroscopy.
  • To elucidate the molecular mechanism underlying the formation of the TGF-beta1/TbetaRII/TbetaRI signaling complex.

Main Methods:

  • Utilized single-molecule force spectroscopy with atomic force microscopy (AFM).
  • Employed AFM tips modified with TGF-beta1 positioned on cells expressing fluorescently tagged TGF-beta receptors.
  • Performed living-cell force measurements combined with fluorescence microscopy.
  • Applied dynamic force spectroscopy to analyze unbinding dynamics under varying AFM loading rates.

Main Results:

  • Coexpression of TbetaRI with TbetaRII significantly enhanced the binding force of TGF-beta1 to its receptors.
  • TbetaRI alone showed no binding affinity for TGF-beta1.
  • TGF-beta1 exhibited more stable binding to the receptor complex after TbetaRI recruitment.
  • Dissociation rate constants and pathways for TGF-beta1-receptor interactions were determined.

Conclusions:

  • TbetaRI plays a critical role in stabilizing the TGF-beta1 signaling complex.
  • The recruitment of TbetaRI is essential for the formation of a stable and functional TGF-beta1 receptor complex.
  • This study provides novel insights into the molecular mechanisms of TGF-beta1 ligand-receptor interactions in living cells.

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