Sponsor: Soichiro Yamada, Ph.D. Biomedical Engineering Mechanotransduction is the process by which cells convert mechanical stimuli into biochemical signals that regulate adhesion, behavior, and fate, yet its molecular mechanisms remain incompletely understood. While current literature focuses on force-induced protein binding, this project investigates proteins that dissociate from actin filaments in response to mechanical stress. To identify candidate proteins, previous experiments used Proximity-Dependent Biotin Identification (BioID) in epithelial cells. After applying large-scale mechanical stretch forces to live cells, mass spectrometry analysis identified the relative abundance of over 1,000 actin-proximal proteins under control and stretch conditions. Four candidate proteins that significantly decreased under stretch conditions were selected for individual study. GFP-tagged candidate proteins were expressed in MDCK cells, revealing colocalization of the MOB4 protein with actin. Live-cell microneedle stretch assays demonstrated force- induced dissociation of MOB4 from actin at cell-to-cell adhesion sites, with minor reassociation with actin when tension was released. Ongoing experiments will focus on investigating the signaling pathway that drives this phenomenon, as well as exploring other candidate proteins. Identifying these force- sensitive interactions will lead to a better understanding of how cells respond to mechanical force, which may explain abnormal cell adhesions in diseases such as cancer. Design Guidelines for 3D-Printed Membrane Bioreactors for Plant Cell Culture

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