期刊
JOURNAL OF CELL SCIENCE
卷 125, 期 9, 页码 2172-2184出版社
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.096214
关键词
Integrins; Kindlins; Keratinocytes
类别
资金
- National Institutes of Health [R03AR054022-01A1, RO1GM-068600, R01GM088240]
- Dermatology Foundation
Integrin-beta 1-null keratinocytes can adhere to fibronectin through integrin alpha v beta 6, but form large peripheral focal adhesions and exhibit defective cell spreading. Here we report that, in addition to the reduced avidity of alpha v beta 6 integrin binding to fibronectin, the inability of integrin beta 6 to efficiently bind and recruit kindlin-2 to focal adhesions directly contributes to these phenotypes. Kindlins regulate integrins through direct interactions with the integrin-beta cytoplasmic tail and keratinocytes express kindlin-1 and kindlin-2. Notably, although both kindlins localize to focal adhesions in wild-type cells, only kindlin-1 localizes to the integrin-beta 6-rich adhesions of integrin-beta 1-null cells. Rescue of these cells with wild-type and chimeric integrin constructs revealed a correlation between kindlin-2 recruitment and cell spreading. Furthermore, despite the presence of kindlin-1, knockdown of kindlin-2 in wild-type keratinocytes impaired cell spreading. Our data reveal unexpected functional consequences of differences in the association of two homologous kindlin isoforms with two closely related integrins, and suggest that despite their similarities, different kindlins are likely to have unique functions.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据