Integrins are dimeric transmembrane receptors that bind the extracellular matrix and allow the cell to adhere and migrate.
In the inactive receptor, the intracellular domains are bound to each other, with the α-subunit inhibiting the β-subunit.
Upon binding to an extracellular ligand, the two domains move apart from each other, triggering binding of intracellular proteins such as Talin.
More on integrins:
De Franceschi et al. Nat. Struc. Mol. Biol. 2016
Talin also bind to PIP2, a important lipid present at sites of integrins activation.
We reconstituted minimal integrins in liposomes and measure Talin binding by high-throughtput FACS analysis.
We found an unexpected, strong synergy between the integrin β-subunit and PIP2 in recruiting Talin (work done in Johanna Ivaska's lab).
Prolif
De Franceschi et al. 2018