Proteins with phophorylated tyrosines (left) match the location of focal adhesions (right).

BURRIDGE

A cell resting on the extracellular matrix (ECM) doesn't just sit there like a football fan in a La-Z-Boy. It develops a deep connection with its substrate. Contact between matrix proteins and integrin receptors in the membrane adjusts the cell's cytoskeleton and shape (Haimovich, et al., 1993), galvanizes survival-promoting pathways, and causes numerous other changes. A 1992 paper by Keith Burridge, Christopher Turner, and Lewis Romer (Burridge et al., 1992) implicated the focal adhesion kinase (FAK) as a key relay for ECM signals. As later studies showed, FAK is a well-connected protein that gets involved in everything from the cell cycle to apoptosis.

By 1992, evidence indicated that ECM proteins pass their messages to the cell by tweaking integrins (see “ECM signals ECM degradation” JCB 172:642),...

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