In case you missed it, methods for the isolation of integrin-associated protein complexes were published in Current Protocols in Cell Biology.

Two protocols for the isolation of adhesion complexes are described.

Adhesion complexes, collections of proteins that work together to allow cells to stick to each other and their surroundings in the body, are important for controlling normal functions of cells. When these complexes don’t form properly in cells, cell adhesion can fail and diseases (such as cancer) can sometimes result.

To assess which proteins make up adhesion complexes, and how these change under different conditions (such as disease), it is necessary to isolate the complexes from cells using biochemical techniques. This is tricky because adhesion complexes are not very stable and they span from the inside to the outside of the cell, making them hard to access in one go.

The two methods described in this chapter of Current Protocols in Cell Biology detail how to stabilise and isolate adhesion complexes from either cells floating in suspension or cells attached to a surface. These isolated proteins can then be identified and quantified using your favourite analytical technique, such as western blotting or mass spectrometry.

This work was supported by the Wellcome Trust, the BBSRC and the University of Manchester.

Jones et al. Isolation of integrin-based adhesion complexes. Curr. Protoc. Cell Biol. 66, 9.8.1–9.8.15 (2015)