Nectins localize Willin to cell-cell junctions

Takashi Ishiuchi, Masatoshi Takeichi

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Willin is a FERM-domain protein, which is related to the Drosophila Expanded, a protein known to be a component of the Hippo signaling pathway. We recently showed that Willin localizes at the apical junctional complex (AJC) in epithelial cells together with Par3 and regulates the contractility of the circumferential actomyosin cables by recruiting aPKC to the AJC. However, it remains unresolved how Willin becomes associated with the AJC. Here, we report that Willin binds to nectins, Ig-family proteins, which also localize at the AJC via their homophilic or heterophilic interactions, and this binding participates in the junctional recruitment of Willin. In addition, we report that the positioning of nectins at the AJC is dependent on their binding to afadin. Thus, our results suggest that the nectin-afadin interaction plays a role in the correct localization of Willin.

Original languageEnglish
Pages (from-to)387-397
Number of pages11
JournalGenes to Cells
Volume17
Issue number5
DOIs
Publication statusPublished - May 1 2012

Fingerprint

Intercellular Junctions
Actomyosin
Epithelial Cells
nectins
Proteins
afadin

All Science Journal Classification (ASJC) codes

  • Genetics
  • Cell Biology

Cite this

Nectins localize Willin to cell-cell junctions. / Ishiuchi, Takashi; Takeichi, Masatoshi.

In: Genes to Cells, Vol. 17, No. 5, 01.05.2012, p. 387-397.

Research output: Contribution to journalArticle

Ishiuchi, Takashi ; Takeichi, Masatoshi. / Nectins localize Willin to cell-cell junctions. In: Genes to Cells. 2012 ; Vol. 17, No. 5. pp. 387-397.
@article{f2990368fb3040719bc5f0f35377fecc,
title = "Nectins localize Willin to cell-cell junctions",
abstract = "Willin is a FERM-domain protein, which is related to the Drosophila Expanded, a protein known to be a component of the Hippo signaling pathway. We recently showed that Willin localizes at the apical junctional complex (AJC) in epithelial cells together with Par3 and regulates the contractility of the circumferential actomyosin cables by recruiting aPKC to the AJC. However, it remains unresolved how Willin becomes associated with the AJC. Here, we report that Willin binds to nectins, Ig-family proteins, which also localize at the AJC via their homophilic or heterophilic interactions, and this binding participates in the junctional recruitment of Willin. In addition, we report that the positioning of nectins at the AJC is dependent on their binding to afadin. Thus, our results suggest that the nectin-afadin interaction plays a role in the correct localization of Willin.",
author = "Takashi Ishiuchi and Masatoshi Takeichi",
year = "2012",
month = "5",
day = "1",
doi = "10.1111/j.1365-2443.2012.01593.x",
language = "English",
volume = "17",
pages = "387--397",
journal = "Genes to Cells",
issn = "1356-9597",
publisher = "Wiley-Blackwell",
number = "5",

}

TY - JOUR

T1 - Nectins localize Willin to cell-cell junctions

AU - Ishiuchi, Takashi

AU - Takeichi, Masatoshi

PY - 2012/5/1

Y1 - 2012/5/1

N2 - Willin is a FERM-domain protein, which is related to the Drosophila Expanded, a protein known to be a component of the Hippo signaling pathway. We recently showed that Willin localizes at the apical junctional complex (AJC) in epithelial cells together with Par3 and regulates the contractility of the circumferential actomyosin cables by recruiting aPKC to the AJC. However, it remains unresolved how Willin becomes associated with the AJC. Here, we report that Willin binds to nectins, Ig-family proteins, which also localize at the AJC via their homophilic or heterophilic interactions, and this binding participates in the junctional recruitment of Willin. In addition, we report that the positioning of nectins at the AJC is dependent on their binding to afadin. Thus, our results suggest that the nectin-afadin interaction plays a role in the correct localization of Willin.

AB - Willin is a FERM-domain protein, which is related to the Drosophila Expanded, a protein known to be a component of the Hippo signaling pathway. We recently showed that Willin localizes at the apical junctional complex (AJC) in epithelial cells together with Par3 and regulates the contractility of the circumferential actomyosin cables by recruiting aPKC to the AJC. However, it remains unresolved how Willin becomes associated with the AJC. Here, we report that Willin binds to nectins, Ig-family proteins, which also localize at the AJC via their homophilic or heterophilic interactions, and this binding participates in the junctional recruitment of Willin. In addition, we report that the positioning of nectins at the AJC is dependent on their binding to afadin. Thus, our results suggest that the nectin-afadin interaction plays a role in the correct localization of Willin.

UR - http://www.scopus.com/inward/record.url?scp=84859916711&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84859916711&partnerID=8YFLogxK

U2 - 10.1111/j.1365-2443.2012.01593.x

DO - 10.1111/j.1365-2443.2012.01593.x

M3 - Article

C2 - 22512338

AN - SCOPUS:84859916711

VL - 17

SP - 387

EP - 397

JO - Genes to Cells

JF - Genes to Cells

SN - 1356-9597

IS - 5

ER -