Kindlin-2 interacts with α-actinin-2 and β1 integrin to maintain the integrity of the Z-disc in cardiac muscles

被引：21
作者：
Qi, Lihua [1 ,2 ,3 ]
Yu, Yu [1 ,2 ,3 ]
Chi, Xiaochun [1 ,2 ,3 ]
Xu, Weizhi [1 ,2 ,3 ]
Lu, Danyu [1 ,2 ,3 ]
Song, Yao [4 ]
Zhang, Youyi [4 ]
Zhang, Hongquan [1 ,2 ,3 ]
机构：
[1] Peking Univ, Key Lab Carcinogenesis & Translat Res, Minist Educ, Hlth Sci Ctr, Beijing 100191, Peoples R China
[2] Peking Univ, State Key Lab Nat & Biomimet Drugs, Hlth Sci Ctr, Beijing 100191, Peoples R China
[3] Peking Univ, Dept Anat Histol & Embryol, Hlth Sci Ctr, Beijing 100191, Peoples R China
[4] Peking Univ, Inst Cardiovasc Res, Hlth Sci Ctr, Beijing 100191, Peoples R China
来源：
FEBS LETTERS | 2015年 / 589卷 / 16期
基金：
北京市自然科学基金; 中国国家自然科学基金;
关键词：
Kindlin-2; alpha-Actinin-2; The Z-disc; Cardiac structure; ALPHA-ACTININ; HYPERTROPHIC CARDIOMYOPATHY; DILATED CARDIOMYOPATHY; INTERCALATED DISCS; PROTEIN; ACTIVATION; COMPLEX; FAMILY; GENE; MYOGENESIS;
D O I：
10.1016/j.febslet.2015.06.022
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Kindlin-2, as an integrin-interacting protein, was known to be required for the maintenance of cardiac structure and function in zebrafish. However, the mechanism remains unclear. We found that Kindlin-2 interacts and colocalizes with alpha-actinin-2 at the Z-disc of mouse cardiac muscles and there Kindlin-2 also interacts with beta 1 integrin. Knockdown of Kindlin-2 influences the association of beta 1 integrin with alpha-actinin-2 and disrupts the structure of the Z-disc and leads to cardiac dysfunction. Our data indicated that Kindlin-2 is a novel alpha-actinin-2-interacting protein and plays an important role in the regulation of cardiac structure and function. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码：2155 / 2162
页数：8
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