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Highly Multiplexed Imaging Uncovers Changes in Compositional Noise within Assembling Focal Adhesions.
Jana Harizanova1, Yessica Fermin2, Rahuman S Malik-Sheriff1
1Department of Systemic Cell Biology, Max Planck Institute of Molecular, Physiology, Dortmund, Germany.
Plos One
|August 13, 2016
Summary
Cell adhesion sites assemble through self-organization. Increased protein density suppresses noise, enabling stable focal adhesion growth and quality control.
Area of Science:
- Cell biology
- Biophysics
Background:
- Integrin adhesome proteins form diverse cell-matrix adhesion sites.
- The self-organization mechanism for correct assembly of these modular sites remains unclear.
Purpose of the Study:
- Investigate the self-organization principles governing focal adhesion assembly.
- Determine how protein interactions lead to ordered adhesion site formation.
Main Methods:
- High-throughput multiplexed imaging of eight proteins and two phosphorylation sites in single focal adhesions.
- Statistical analysis of protein density variances and correlations.
- Artificial neural network analysis to predict protein levels.
Main Results:
- Protein density variances decrease while correlations increase during focal adhesion assembly, indicating noise reduction.
- These changes correlate with focal adhesion area and internal density.
- Artificial neural networks predict paxillin and zyxin levels better when considering multiple components.
Conclusions:
- Focal adhesion assembly involves noise suppression facilitated by increased internal protein densities.
- A feedback loop between density increase and noise suppression enables stable, quality-controlled assembly of focal adhesions.
