Poster abstracts
Poster number 81 submitted by Benedict Hui
Impact of the high flexibility of the cadherin-catenin-vinculin complex on F-actin attachment
Benedict S. F. Hui (Biophysics Graduate Program), Xiaolin Cheng (Division of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, The Ohio State University)
Abstract:
Adherens junctions (AJs) are where cells adhere together to maintain tissue integrity and regulate signaling between cells and tumor progression. The core component of AJ is the cadherin-catenin complex and the cytoskeletal actin filament (F-actin). Vinculin, a cytoskeletal protein, is recruited and activated by AJ to modulate cell adhesiveness by continually breaking and remaking adhesive bonds with neighboring cells. In this research, molecular dynamics (MD) simulations were used to study how the formation of the cadherin-catenin-vinculin complex (VABE complex) through vinculin recruitment leads to the deformation of &alpha-catenin and results in its high flexibility. In addition, we investigated how such high flexibility enables the exposure of both &alpha-catenin and vinculin actin-binding domain (ABD), which affects their attachments to F-actin. The root-mean-square fluctuation (RMSF) analysis shows that the recruitment of vinculin by &alpha-catenin increases its flexibility due to the unfolding of its M1 domain when recruiting vinculin. The solvent accessible surface area (SASA) analysis shows this high flexibility enables the exposure of both &alpha-catenin ABD and vinculin ABD and affects their chance to attach to F-actin.
Keywords: cadherin, catenin, vinculin