CLASP2 interacts with p120-catenin and governs microtubule dynamics at adherens junctions

Marta N Shahbazi, Diego Megias, Carolina Epifano, Anna Akhmanova, Gregg G Gundersen, Elaine Fuchs, Mirna Perez-Moreno

22 Citations (Scopus)

Abstract

Classical cadherins and their connections with microtubules (MTs) are emerging as important determinants of cell adhesion. However, the functional relevance of such interactions and the molecular players that contribute to tissue architecture are still emerging. In this paper, we report that the MT plus end-binding protein CLASP2 localizes to adherens junctions (AJs) via direct interaction with p120-catenin (p120) in primary basal mouse keratinocytes. Reductions in the levels of p120 or CLASP2 decreased the localization of the other protein to cell-cell contacts and altered AJ dynamics and stability. These features were accompanied by decreased MT density and altered MT dynamics at intercellular junction sites. Interestingly, CLASP2 was enriched at the cortex of basal progenitor keratinocytes, in close localization to p120. Our findings suggest the existence of a new mechanism of MT targeting to AJs with potential functional implications in the maintenance of proper cell-cell adhesion in epidermal stem cells.

Original languageEnglish
JournalJournal of Cell Biology
Volume203
Issue number6
Pages (from-to)1043-1061
Number of pages19
ISSN0021-9525
DOIs
Publication statusPublished - 23 Dec 2013
Externally publishedYes

Keywords

  • Adherens Junctions
  • Animals
  • Catenins
  • Cell Adhesion
  • HEK293 Cells
  • Humans
  • Keratinocytes
  • Mice
  • Microtubule-Associated Proteins
  • Microtubules
  • Models, Biological
  • Journal Article
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

Fingerprint

Dive into the research topics of 'CLASP2 interacts with p120-catenin and governs microtubule dynamics at adherens junctions'. Together they form a unique fingerprint.

Cite this