title: Recruitment of β-catenin to N-cadherin is necessary for smooth muscle contraction.
abstract: β-Catenin is a key component that connects transmembrane cadherin with the actin cytoskeleton at the cell-cell interface. However, the role of the β-catenin/cadherin interaction in smooth muscle has not been well characterized. Here stimulation with acetylcholine promoted the recruitment of β-catenin to N-cadherin in smooth muscle cells/tissues. Knockdown of β-catenin by lentivirus-mediated shRNA attenuated smooth muscle contraction. Nevertheless, myosin light chain phosphorylation at Ser-19 and actin polymerization in response to contractile activation were not reduced by β-catenin knockdown. In addition, the expression of the β-catenin armadillo domain disrupted the recruitment of β-catenin to N-cadherin. Force development, but not myosin light chain phosphorylation and actin polymerization, was reduced by the expression of the β-catenin armadillo domain. Furthermore, actin polymerization and microtubules have been implicated in intracellular trafficking. In this study, the treatment with the inhibitor latrunculin A diminished the interaction of β-catenin with N-cadherin in smooth muscle. In contrast, the exposure of smooth muscle to the microtubule depolymerizer nocodazole did not affect the protein-protein interaction. Together, these findings suggest that smooth muscle contraction is mediated by the recruitment of β-catenin to N-cadherin, which may facilitate intercellular mechanotransduction. The association of β-catenin with N-cadherin is regulated by actin polymerization during contractile activation.
authors.affiliation: From the Center for Cardiovascular Sciences, Albany Medical College, Albany, New York 12208.
authors.forename: Tao
authors.initials: T
authors.lastname: Wang
authors.affiliation: From the Center for Cardiovascular Sciences, Albany Medical College, Albany, New York 12208.
authors.forename: Ruping
authors.initials: R
authors.lastname: Wang
authors.affiliation: From the Center for Cardiovascular Sciences, Albany Medical College, Albany, New York 12208.
authors.forename: Rachel A
authors.initials: RA
authors.lastname: Cleary
authors.affiliation: From the Center for Cardiovascular Sciences, Albany Medical College, Albany, New York 12208.
authors.forename: Olivia J
authors.initials: OJ
authors.lastname: Gannon
authors.affiliation: From the Center for Cardiovascular Sciences, Albany Medical College, Albany, New York 12208 tangd@mail.amc.edu.
authors.forename: Dale D
authors.initials: DD
authors.lastname: Tang
mesh_terms: D000199:Actins / Q000378:metabolism; D015820:Cadherins / Q000378:metabolism*; D002478:Cells, Cultured; D006801:Humans; D040542:Mechanotransduction, Cellular; D008870:Microtubules / Q000378:metabolism; D009119:Muscle Contraction; D009130:Muscle, Smooth / Q000166:cytology / Q000378:metabolism / Q000502:physiology*; D058105:Polymerization; D051176:beta Catenin / Q000378:metabolism*
chemical_list: D000199:Actins; D015820:Cadherins; D051176:beta Catenin
keywords: Adherens Junction; Cytoskeleton; Excitation-Contraction Coupling (E-C Coupling); Signal Transduction; Smooth Muscle