Abstract
The kindlin family of peripheral membrane proteins are a key component of the cytosolic side of the integrin transmembrane receptor complexes. Kindlin-2 (K2), the member of the family most ubiquitously expressed in humans, acts as a hub for numerous protein-protein interactions and is regulated in part through its binding to membranes containing phosphatidylinositol phosphates (PIPs) via two dedicated PIP binding domains. Our lab uses solid-state NMR and molecular dynamics simulations to probe the K2-lipid interface and answer questions about how lipid binding affects the structure and dynamics of K2.
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