Role of Multiple Bonds Between the Single Cell Adhesion Molecules, Nectin and Cadherin, Revealed by High Sensitive Force Measurements

Tsukasaki, Yoshikazu; Kitamura, Kazuhiro; Shimizu, Kazuya; Iwane, Atsuko H.; Takai, Yoshimi; Yanagida, Toshio

doi:10.1016/j.jmb.2006.12.022

Cited by 43 publications

(32 citation statements)

References 51 publications

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“…To evaluate the binding properties of these fragments, we measured the dissociation processes, because the association processes are difficult to analyze due to the self-association of the molecules as well as the presence of multiple bound states of cadherins (19,20). The dissociation process of E-cadherin matched well with the multiple exponential fits as previously observed (20), and this was also the case for Dachsous1 and Fat4 (Fig. 4C and Fig.…”

Section: Heterophilic Interactions Between Fat4 and Dachsous1 Via Theirsupporting

confidence: 79%

Giant cadherins Fat and Dachsous self-bend to organize properly spaced intercellular junctions

Tsukasaki¹,

Miyazaki

Matsumoto

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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The cadherins Fat and Dachsous regulate cell polarity and proliferation via their heterophilic interactions at intercellular junctions. Their ectodomains are unusually large because of repetitive extracellular cadherin (EC) domains, which raises the question of how they fit in regular intercellular spaces. Cadherins typically exhibit a linear topology through the binding of Ca 2+ to the linker between the EC domains. Our electron-microscopic observations of mammalian Fat4 and Dachsous1 ectodomains, however, revealed that, although their N-terminal regions exhibit a linear configuration, the C-terminal regions are kinked with multiple hairpin-like bends.

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Section: Heterophilic Interactions Between Fat4 and Dachsous1 Via Theirsupporting

confidence: 79%

Giant cadherins Fat and Dachsous self-bend to organize properly spaced intercellular junctions

Tsukasaki¹,

Miyazaki

Matsumoto

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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“…It remains elusive how the strand-dimer model can explain the three force states obtained in our experiments, and that of others, with recombinant dimers -a conformation that does not exist in this model but that has been shown to be important for cadherin function (Chen et al, 2005). Very recently, force data obtained with the highly sensitive 'intermolecular force microscopy', revealed three to four force peaks for the singlemolecule interaction between E-cadherin:Fc chimeras (Tsukasaki et al, 2007). The authors present an alternative model that may be congruent with both the 'strand-dimer' model and the EC interdigitation model (Fig.…”

Section: Discussionmentioning

confidence: 53%

Fibrogenic fibroblasts increase intercellular adhesion strength by reinforcing individual OB-cadherin bonds

Pittet

Lee

Kulik

et al. 2008

Journal of Cell Science

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depolymerization reduces single-bond strength to the level of cadherin constructs missing the cytoplasmic domain. Hence, fibroblasts reinforce intercellular contacts by: (1) switching from N-to OB-cadherin expression; (2) increasing the strength of single-molecule bonds in three distinct steps; and (3) actinpromoted intrinsic activation of cadherin extracellular binding. We propose that this plasticity adapts fibroblast adhesions to the changing mechanical microenvironment of tissue under remodeling. Supplementary material available online at

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“…Prior biophysical studies identified multiple bonds between cadherin ectodomains that require different domains (Bayas et al, 2006;Bibert et al, 2002;Chappuis-Flament et al, 2001;Chien et al, 2008;Perret et al, 2004;Shi et al, 2008;Sivasankar et al, 1999;Sivasankar et al, 2001;Tsukasaki et al, 2007;Zhu et al, 2003). All five EC domains are needed to recapitulate the kinetic signature of the intact protein .…”

Section: Discussionmentioning

confidence: 99%

Cadherin Point Mutations Alter Cell Sorting and Modulate GTPase Signaling

Tabdili

Barry

Langer

et al. 2012

Journal of Cell Science

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SummaryThis study investigated the impact of cadherin binding differences on both cell sorting and GTPase activation. The use of N-terminal domain point mutants of Xenopus C-cadherin enabled us to quantify binding differences and determine their effects on cadherindependent functions without any potential complications arising as a result of differences in cytodomain interactions. Dynamic cell-cell binding measurements carried out with the micropipette manipulation technique quantified the impact of these mutations on the twodimensional binding affinities and dissociation rates of cadherins in the native context of the cell membrane. Pairwise binding affinities were compared with in vitro cell-sorting specificity and ligation-dependent GTPase signaling. Two-dimensional affinity differences greater than five-fold correlated with cadherin-dependent in vitro cell segregation, but smaller differences failed to induce cell sorting.Comparison of the binding affinities with GTPase signaling amplitudes further demonstrated that differential binding also proportionally modulates intracellular signaling. These results show that differential cadherin affinities have broader functional consequences than merely controlling cell-cell cohesion.

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Role of Multiple Bonds Between the Single Cell Adhesion Molecules, Nectin and Cadherin, Revealed by High Sensitive Force Measurements

Cited by 43 publications

References 51 publications

Giant cadherins Fat and Dachsous self-bend to organize properly spaced intercellular junctions

Giant cadherins Fat and Dachsous self-bend to organize properly spaced intercellular junctions

Fibrogenic fibroblasts increase intercellular adhesion strength by reinforcing individual OB-cadherin bonds

Cadherin Point Mutations Alter Cell Sorting and Modulate GTPase Signaling

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