Publication Date:
2014-11-02
Description:
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 alphaE-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.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4364042/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4364042/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buckley, Craig D -- Tan, Jiongyi -- Anderson, Karen L -- Hanein, Dorit -- Volkmann, Niels -- Weis, William I -- Nelson, W James -- Dunn, Alexander R -- 1DP2OD007078/OD/NIH HHS/ -- DP2 OD007078/OD/NIH HHS/ -- GM35527/GM/NIGMS NIH HHS/ -- GM56169/GM/NIGMS NIH HHS/ -- P01 GM098412/GM/NIGMS NIH HHS/ -- P01GM098412/GM/NIGMS NIH HHS/ -- R01 GM035527/GM/NIGMS NIH HHS/ -- R01 GM056169/GM/NIGMS NIH HHS/ -- T32 GM008294/GM/NIGMS NIH HHS/ -- U01 GM094663/GM/NIGMS NIH HHS/ -- U01GM094663/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2014 Oct 31;346(6209):1254211. doi: 10.1126/science.1254211.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, Stanford University, Stanford, CA 94305, USA. ; Biophysics Program, Stanford University, Stanford, CA 94305, USA. ; Bioinformatics and Structural Systems Biology Program, Sanford-Burnham Medical Research Institute, La Jolla, CA 92037, USA. ; Biophysics Program, Stanford University, Stanford, CA 94305, USA. Department of Structural Biology, Stanford University, Stanford, CA 94305, USA. Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA. alex.dunn@stanford.edu wjnelson@stanford.edu bill.weis@stanford.edu. ; Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA. Department of Biology, Stanford University, Stanford, CA 94305, USA. alex.dunn@stanford.edu wjnelson@stanford.edu bill.weis@stanford.edu. ; Department of Chemical Engineering, Stanford University, Stanford, CA 94305, USA. Biophysics Program, Stanford University, Stanford, CA 94305, USA. Stanford Cardiovascular Institute, Stanford University, Stanford, CA 94305, USA. alex.dunn@stanford.edu wjnelson@stanford.edu bill.weis@stanford.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25359979" target="_blank"〉PubMed〈/a〉
Keywords:
Actin Cytoskeleton/*metabolism
;
Actins/*metabolism
;
Adherens Junctions/*metabolism
;
Caco-2 Cells
;
Cadherins/*metabolism
;
Catenins/*metabolism
;
Cell Adhesion
;
Humans
;
*Mechanotransduction, Cellular
;
Protein Binding
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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