TY - JOUR T1 - Talin-KANK1 interaction controls the recruitment of cortical microtubule stabilizing complexes to focal adhesions JF - bioRxiv DO - 10.1101/055210 SP - 055210 AU - Benjamin P. Bouchet AU - Rosemarie E. Gough AU - Dieudonnée van de Willige AU - York-Christoph Ammon AU - Harm Post AU - Guillaume Jacquemet AU - A.F. Maarten Altelaar AU - Albert J.R. Heck AU - Benjamin T. Goult AU - Anna Akhmanova Y1 - 2016/01/01 UR - http://biorxiv.org/content/early/2016/05/24/055210.abstract N2 - The cross-talk between dynamic microtubules and integrin-based adhesions to the extracellular matrix plays a crucial role in cell polarity and migration. Microtubules regulate the turnover of adhesion sites, and, in turn, focal adhesions promote cortical microtubule capture and stabilization in their vicinity, but the underlying mechanism is unknown. Here, we show that cortical microtubule stabilization sites containing CLASPs, KIF21A, LL5P and liprins are recruited to focal adhesions by the adaptor protein KANK1, which directly interacts with the major adhesion component, talin. Structural studies showed that the conserved KN domain in KANK1 binds to the talin rod domain R7. Perturbation of this interaction, including a single point mutation in talin, which disrupts KANK1 binding but not the talin function in adhesion, abrogates the association of microtubule-stabilizing complexes with focal adhesions. We propose that the talin-KANK1 interaction links the two macromolecular assemblies that control cortical attachment of actin fibers and microtubules. ER -