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 language | English |
|---|---|
| Pages (from-to) | 387-397 |
| Number of pages | 11 |
| Journal | Genes to Cells |
| Volume | 17 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - May 1 2012 |
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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 journal › Article
}
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.
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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 -