Anchorage of Microtubule Minus Ends to Adherens Junctions Regulates Epithelial Cell-Cell Contacts

• Published in: Cell Vol. 135; no. 5; pp. 948 - 959
• Main Authors: Meng, Wenxiang, Mushika, Yoshimi, Ichii, Tetsuo, Takeichi, Masatoshi
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 28.11.2008
• Subjects: Adherens Junctions - metabolism; Animals; Carrier Proteins - metabolism; Catenins; Cell Adhesion Molecules - metabolism; Cell Communication; Cell Line, Tumor; CELLBIO; DEVBIO; Epithelial Cells - cytology; Epithelial Cells - metabolism; Humans; Kinesin - metabolism; Mice; Microtubules - metabolism; Phosphoproteins - metabolism; Protein Interaction Mapping; SIGNALING; CELLBIO; DEVBIO; SIGNALING
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/j.cell.2008.09.040

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.