Symmetric exchange of multi-protein building blocks between stationary focal adhesions and the cytosol

Elife. 2014 Jun 3;3:e02257. doi: 10.7554/eLife.02257.


How can the integrin adhesome get self-assembled locally, rapidly, and correctly as diverse cell-matrix adhesion sites? Here, we investigate this question by exploring the cytosolic state of integrin-adhesome components and their dynamic exchange between adhesion sites and cytosol. Using fluorescence cross-correlation spectroscopy (FCCS) and fluorescence recovery after photobleaching (FRAP) we found that the integrin adhesome is extensively pre-assembled already in the cytosol as multi-protein building blocks for adhesion sites. Stationary focal adhesions release symmetrically the same types of protein complexes that they recruit, thereby keeping the cytosolic pool of building blocks spatiotemporally uniform. We conclude a model in which multi-protein building blocks enable rapid and modular self-assembly of adhesion sites and symmetric exchange of these building blocks preserves their specifications and thus the assembly logic of the system.DOI:

Keywords: cell adhesion; focal adhesions; integrin adhesome; protein complexes; self assembly.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cells, Cultured
  • Cytosol / metabolism*
  • Focal Adhesions / metabolism*
  • Proteins / metabolism*
  • Rats
  • Spectrometry, Fluorescence / methods


  • Proteins

Grant support

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.