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

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 fluorescenc...

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Bibliographic Details
Published in:eLife 2014-06, Vol.3, p.e02257-e02257
Main Authors: Hoffmann, Jan-Erik, Fermin, Yessica, Stricker, Ruth Lo, Ickstadt, Katja, Zamir, Eli
Format: Article
Language:English
Subjects:
Animals
Binding sites
cell adhesion
Cell Biology
Cells, Cultured
Cytosol
Cytosol - metabolism
Enzymes
Fluorescence recovery after photobleaching
focal adhesion
Focal Adhesions - metabolism
integrin adhesome
Mutagenesis
Photobleaching
protein complex
Proteins
Proteins - metabolism
Rats
Self-assembly
Spectrometry, Fluorescence - methods
Spectroscopy
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Summary: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: http://dx.doi.org/10.7554/eLife.02257.001.
ISSN:2050-084X
2050-084X
DOI:10.7554/elife.02257