Cells of the body are constantly communicating with their surroundings. This integration of cells with their local environment is mediated by proteins on the surface of cells called integrin adhesion receptors. But how these proteins precisely control normal cellular functions is not well understood. In fact, it turns out to be extremely complex.

In new work, this complexity of cellular signalling is analysed. Distilling down the deluge of data allowed us to discover a key collection of components that congregate at sites of cell adhesion. These proteins play important roles in allowing cells to sense their surroundings, move and survive. When these processes go wrong, diseases like cancer can develop.

Our work is also featured on the cover of this month’s issue of Nature Cell Biology, with an image by Ed Horton showing all the proteins we analysed. See if you can spot your favourite adhesion protein!

Nature Cell Biology cover, 2015, vol. 17 (no. 12) // Image by Ed Horton

Nature Cell Biology cover, 2015, vol. 17 (no. 12)

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A press release has been issued by Cancer Research UK about a paper from the University of Edinburgh on the protein focal adhesion kinase (or FAK) and how it modulates the immune system in cancer to allow tumour cells to grow.

A class of experimental drug treatments already in clinical trials could also help the body’s immune system to fight cancer.

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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.

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When cells adhere to and interact with their surroundings in tissues, they generate and transmit molecular signals that control how the cells behave, such as whether they move, grow or divide. Molecules that carry these signals are often modified temporarily to switch the signals on or off. One important type of biochemical modification is phosphorylation, which plays a role in many cell signalling processes, including cell adhesion.

Adhesion signalling molecules activated by phosphorylation // Image by Adam Byron

Adhesion signalling molecules activated by phosphorylation

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Integrins are a family of adhesion proteins that interact with and sense neighbouring cells and the surrounding extracellular environment. They project from the surface of cells like antennae and transmit signals back and forth between the cell and its surroundings – this signalling controls a wide range of important cellular functions.

A network of cell adhesion proteins in the constellation of the proteome // Image by Adam Byron

A network of cell adhesion proteins in the constellation of the proteome

Amazingly, to signal, the integrin molecules change shape in the cell membrane, twisting from a compact “inactive” position to an extended “active” position. Depending on the shape of the integrins, different proteins attach to them to assist in the signalling process. But which proteins bind to different conformations of integrins, and how does this change the behaviour of a cell in response to its surroundings?

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