Highly Multiplexed Imaging Uncovers Changes in Compositional Noise within Assembling Focal Adhesions.

ABSTRACT: Integrin adhesome proteins bind each other in alternative manners, forming within the cell diverse cell-matrix adhesion sites with distinct properties. An intriguing question is how such modular assembly of adhesion sites is achieved correctly solely by self-organization of their components. Here we address this question using high-throughput multiplexed imaging of eight proteins and two phosphorylation sites in a large number of single focal adhesions. We found that during the assembly of focal adhesions the variances of protein densities decrease while the correlations between them increase, suggesting reduction in the noise levels within these structures. These changes correlate independently with the area and internal density of focal adhesions, but not with their age or shape. Artific

SUBMITTER: Harizanova J 

PROVIDER: S-EPMC4982658 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature