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Tension Gauge Tether Probes for Quantifying Growth Factor Mediated Integrin Mechanics and Adhesion
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Regulated RIAM-Talin Engagement Controls Adhesion Stability and Mechanical Output.

Nikhil Mittal1,2, Ho-Sup Lee3, Mark H Ginsberg3

  • 1Department of Biomedical Engineering, Michigan Technological University, Houghton, MI, USA.

Biorxiv : the Preprint Server for Biology
|February 6, 2026
PubMed
Summary
This summary is machine-generated.

Prolonging RIAM-talin interactions enhances integrin activation and cell traction forces by altering adhesion dynamics. Rap1 signaling is crucial for optimal adhesion turnover and force transmission.

Keywords:
Focal adhesionRIAMRap1phosphoinositidestalin-1traction force

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Mechanobiology

Background:

  • RIAM (Rap1-GTP-interacting adaptor molecule) is key for integrin activation, linking Rap1 to talin-1.
  • RIAM's typical localization at nascent adhesions suggests its engagement duration influences cell adhesion dynamics.
  • The precise impact of sustained RIAM-talin engagement on adhesion plasticity and force transmission is not fully understood.

Purpose of the Study:

  • To investigate how the duration of RIAM-talin engagement affects cell adhesion dynamics and force transmission.
  • To explore the role of sustained RIAM-talin association in reprogramming adhesion properties.

Main Methods:

  • Utilized a RIAM chimera engineered to enforce sustained talin association by replacing its native talin-binding site.
  • Redistributed RIAM modules to mature adhesions using the Kank2 talin-binding motif.
  • Analyzed integrin activation, adhesion assembly/disassembly rates, adhesion lifetime, nascent adhesion nucleation, cellular traction forces, and Rap1 dependency.

Main Results:

  • The RIAM chimera enhanced integrin activation and accelerated both adhesion assembly and disassembly.
  • Adhesion lifetime was reduced, while the fraction of RIAM-nucleated nascent adhesions increased.
  • Cellular traction forces were elevated, with integrin activation being largely Rap1-independent, but Rap1 binding essential for optimal turnover and force generation.

Conclusions:

  • Sustained talin engagement with RIAM is sufficient to reprogram adhesion dynamics and enhance cell traction.
  • Rap1 plays a separable role in coordinating force transmission downstream of integrin activation.
  • Regulating RIAM residence time and engagement mode at talin is critical for controlling adhesion plasticity and mechanotransduction.