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

• Main Authors: Jan-Erik Hoffmann, Yessica Fermin, Ruth LO Stricker, Katja Ickstadt, Eli Zamir
• Format: Article
• Language: English
• Published: eLife Sciences Publications Ltd 2014-06-01
• Series: eLife
• Subjects: integrin adhesome; focal adhesion; cell adhesion; protein complex; self assembly
• Online Access: https://elifesciences.org/articles/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.