May 24, 2016

Talin-KANK1 interaction controls the recruitment of cortical microtubule stabilizing complexes to focal adhesions.

BioRxiv : the Preprint Server for Biology
Benjamin P. BouchetAnna Akhmanova

Abstract

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, LL5beta 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.

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Mentioned in this Paper

Study
KIF21A protein, human
TLN1
Cross-talk
Actins
Cortical Microtubule
Complex (molecular entity)
Extracellular Matrix
Focal Adhesions
PHLDB2

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