The minimal cadherin-catenin complex binds to actin filaments under force

被引:454
作者
Buckley, Craig D. [1 ]
Tan, Jiongyi [2 ]
Anderson, Karen L. [3 ]
Hanein, Dorit [3 ]
Volkmann, Niels [3 ]
Weis, William I. [2 ,4 ,5 ]
Nelson, W. James [5 ,6 ]
Dunn, Alexander R. [1 ,2 ,7 ]
机构
[1] Stanford Univ, Dept Chem Engn, Stanford, CA 94305 USA
[2] Stanford Univ, Biophys Program, Stanford, CA 94305 USA
[3] Sanford Burnham Med Res Inst, Bioinformat & Struct Syst Biol Program, La Jolla, CA 92037 USA
[4] Stanford Univ, Dept Biol Struct, Stanford, CA 94305 USA
[5] Stanford Univ, Dept Mol & Cellular Physiol, Stanford, CA 94305 USA
[6] Stanford Univ, Dept Biol, Stanford, CA 94305 USA
[7] Stanford Univ, Stanford Cardiovascular Inst, Stanford, CA 94305 USA
关键词
CELL-ADHESION MOLECULES; ALPHA-E-CATENIN; BETA-CATENIN; CATCH BONDS; ADHERENS JUNCTIONS; F-ACTIN; SLIP BONDS; VINCULIN; PROTEIN; DISSOCIATION;
D O I
10.1126/science.1254211
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
070301 [无机化学]; 070403 [天体物理学]; 070507 [自然资源与国土空间规划学]; 090105 [作物生产系统与生态工程];
摘要
Linkage between the adherens junction (AJ) and the actin cytoskeleton is required for tissue development and homeostasis. In vivo findings indicated that the AJ proteins E-cadherin, beta-catenin, and the filamentous (F)-actin binding protein alpha E-catenin form a minimal cadherin-catenin complex that binds directly to F-actin. Biochemical studies challenged this model because the purified cadherin-catenin complex does not bind F-actin in solution. Here, we reconciled this difference. Using an optical trap-based assay, we showed that the minimal cadherin-catenin complex formed stable bonds with an actin filament under force. Bond dissociation kinetics can be explained by a catch-bond model in which force shifts the bond from a weakly to a strongly bound state. These results may explain how the cadherin-catenin complex transduces mechanical forces at cell-cell junctions.
引用
收藏
页码:600 / +
页数:9
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