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

Benjamin P Bouchet, Rosemarie E Gough, York-Christoph Ammon, Dieudonnée van de Willige, Harm Post, Guillaume Jacquemet, Af Maarten Altelaar, Albert Jr Heck, Benjamin T Goult*, Anna Akhmanova*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

108 Citations (Web of Science)

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 the 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, LL5β 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.

Original languageEnglish
Article numbere18124
JournalElife
Volume5
DOIs
Publication statusPublished - 13 Jul 2016
Externally publishedYes

Keywords

  • Adaptor Proteins, Signal Transducing
  • Cytoskeletal Proteins
  • Focal Adhesions/metabolism
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Microtubules/metabolism
  • Talin/metabolism
  • Tumor Suppressor Proteins/metabolism

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