title: Homophilic interaction and deformation of E-cadherin and cadherin 7 probed by single molecule force spectroscopy.
abstract: Cadherin-mediated adhesion plays a crucial role in multicellular organisms. Dysfunction within this adhesion system has major consequences in many pathologies, including cancer invasion and metastasis. However, mechanisms controlling cadherin recognition and adhesive strengthening are only partially understood. Here, we investigated the homophilic interactions and mechanical stability of the extracellular (EC) domains of E-cadherin and cadherin 7 using atomic force microscopy and magnetic tweezers. Besides exhibiting stronger interactions, E-cadherin also showed more efficient force-induced self-strengthening of interactions than cadherin 7. In addition, the distributions of the unbinding forces for both cadherins partially overlap with those of the unfolding forces, indicating that partial unfolding/deformation of the cadherin EC domains may take place during their homophilic interactions. These conformational changes may be involved in cadherins physiology function and contribute to the significant differences in adhesive strength mediated by type I and type II cadherins.
authors.affiliation: College of Physics, Chongqing University, No.55 Daxuecheng South Rd., Shapingba, Chongqing 401331, China; Department of Physics, National University of Singapore, 2 Science Drive 3, Singapore 117542, Singapore; Mechanobiology Institute, National University of Singapore, 5A Engineering Drive 1, Singapore 117411, Singapore.
authors.forename: Fei
authors.initials: F
authors.lastname: Wu
authors.affiliation: Institute of Molecular and Cell Biology, Proteos, Singapore 138673, Singapore.
authors.forename: Prashant
authors.initials: P
authors.lastname: Kumar
authors.affiliation: Mechanobiology Institute, National University of Singapore, 5A Engineering Drive 1, Singapore 117411, Singapore.
authors.forename: Chen
authors.initials: C
authors.lastname: Lu
authors.affiliation: Institut Curie CNRS144, Paris 75005, France.
authors.forename: Ahmed
authors.initials: A
authors.lastname: El Marjou
authors.affiliation: College of Physics, Chongqing University, No.55 Daxuecheng South Rd., Shapingba, Chongqing 401331, China; Department of Physics, National University of Singapore, 2 Science Drive 3, Singapore 117542, Singapore.
authors.forename: Wu
authors.initials: W
authors.lastname: Qiu
authors.affiliation: Mechanobiology Institute, National University of Singapore, 5A Engineering Drive 1, Singapore 117411, Singapore; Department of Bioengineering, National University of Singapore, 9 Engineering Drive 1, Singapore 117576, Singapore.
authors.forename: Chwee Teck
authors.initials: CT
authors.lastname: Lim
authors.affiliation: Institute of Molecular and Cell Biology, Proteos, Singapore 138673, Singapore; Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, 8 Medical Drive, Singapore 117597, Singapore.
authors.forename: Jean Paul
authors.initials: JP
authors.lastname: Thiery
authors.affiliation: College of Physics, Chongqing University, No.55 Daxuecheng South Rd., Shapingba, Chongqing 401331, China; Department of Physics, National University of Singapore, 2 Science Drive 3, Singapore 117542, Singapore; Mechanobiology Institute, National University of Singapore, 5A Engineering Drive 1, Singapore 117411, Singapore. Electronic address: phyliurc@cqu.edu.cn.
authors.forename: Ruchuan
authors.initials: R
authors.lastname: Liu
mesh_terms: D015820:Cadherins / Q000737:chemistry / Q000378:metabolism*; D002448:Cell Adhesion; D008280:Magnetics; D055595:Mechanical Phenomena; D018625:Microscopy, Atomic Force; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D058767:Protein Unfolding
chemical_list: D015820:Cadherins
keywords: Atomic force microscopy; Cell adhesion; Force spectroscopy; Magnetic tweezers