Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts

Cell. 2008 Nov 28;135(5):948-59. doi: 10.1016/j.cell.2008.09.040.

Abstract

Epithelial cells contain noncentrosomal microtubules (MTs), whose minus ends are oriented apically. In contrast with the well-known interactions of the minus ends with the centrosome, little is known about the termination site of the noncentrosomal minus ends. Here we show that a population of MT minus ends is anchored at the zonula adherens (ZA), the apical-most part of the cadherin-based adherens junction, via a protein that we have termed Nezha. We initially identified PLEKHA7 as a ZA component and subsequently detected Nezha as a partner for PLEKHA7. Nezha bound MTs at their minus ends and tethered them to the ZA. Furthermore, we found that a minus end-directed motor, KIFC3, was concentrated at the ZA in a PLEKHA7/Nezha/MT-dependent manner; and depletion of any of these proteins resulted in disorganization of the ZA. We propose that the PLEKHA7/Nezha/MT complex regulates the ZA integrity by recruiting KIFC3 to this junctional site.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adherens Junctions / metabolism*
  • Animals
  • Carrier Proteins / metabolism
  • Catenins
  • Cell Adhesion Molecules / metabolism
  • Cell Communication*
  • Cell Line, Tumor
  • Delta Catenin
  • Epithelial Cells / cytology*
  • Epithelial Cells / metabolism
  • Humans
  • Kinesins / metabolism
  • Mice
  • Microtubules / metabolism*
  • Phosphoproteins / metabolism
  • Protein Interaction Mapping

Substances

  • Carrier Proteins
  • Catenins
  • Cell Adhesion Molecules
  • Kifc3 protein, mouse
  • PLEKHA7 protein, human
  • Phosphoproteins
  • Kinesins
  • Delta Catenin