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• W2091216980 endingPage "e0122886" @default.
• W2091216980 startingPage "e0122886" @default.
• W2091216980 abstract "Tissues and organs undergo constant physical perturbations and individual cells must respond to mechanical forces to maintain tissue integrity. However, molecular interactions underlying mechano-transduction are not fully defined at cell-cell junctions. This is in part due to weak and transient interactions that are likely prevalent in force-induced protein complexes. Using in situ proximal biotinylation by the promiscuous biotin ligase BirA tagged to α-catenin and a substrate stretch cell chamber, we sought to identify force-dependent molecular interactions surrounding α-catenin, an actin regulator at the sites of cadherin mediated cell-cell adhesion. While E-cadherin, β-catenin, vinculin and actin localize with α-catenin at cell-cell contacts in immuno-fluorescent staining, only β-catenin and plakoglobin were biotinylated, suggesting that this proximal biotinylation is limited to the molecules that are in the immediate vicinity of α-catenin. In mechanically stretched samples, increased biotinylation of non-muscle myosin IIA, but not myosin IIB, suggests close spatial proximity between α-catenin and myosin IIA during substrate stretching. This force-induced biotinylation diminished as myosin II activity was inhibited by blebbistatin. Taken together, this promising technique enables us to identify force sensitive complexes that may be essential for mechano-responses in force bearing cell adhesion." @default.
• W2091216980 created "2016-06-24" @default.
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• W2091216980 date "2015-03-25" @default.
• W2091216980 modified "2023-09-26" @default.
• W2091216980 title "Force Dependent Biotinylation of Myosin IIA by α-Catenin Tagged with a Promiscuous Biotin Ligase" @default.
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• W2091216980 doi "https://doi.org/10.1371/journal.pone.0122886" @default.
• W2091216980 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4373798" @default.
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