A5013041896- Cellular transport and secretion
- Phagocytosis and Immune Regulation
- Cell death mechanisms and regulation
- Cellular Mechanics and Interactions
- Lipid Membrane Structure and Behavior
- Photochromic and Fluorescence Chemistry
- Erythrocyte Function and Pathophysiology
- Cell Adhesion Molecules Research
The Ohio State University
2021-2024
Abstract The transmembrane death receptor Fas transduces apoptotic signals upon binding its ligand, FasL. Although is highly expressed in cancer cells, insufficient cell surface expression desensitizes cells to Fas-induced apoptosis. Here, we show that the increase microaggregate formation on plasma membrane response inhibition of endocytosis sensitizes We used a clinically accessible Rho-kinase inhibitor, fasudil, reduces dynamics by increasing tension. In combination with exogenous soluble...
Abstract Fas (CD95/APO-1) is a transmembrane death receptor that transduces apoptotic signals upon binding to its ligand and assembling into death-inducing signaling complex (DISC) ( 1, 2 ). Intracellular trafficking of receptors, including recycling from endosomes the plasma membrane, plays vital role in ligand-induced assembly DISC 3, 4 Although highly expressed tumor cells 5, 6 ), insufficient expression these receptors on cell surface makes cancer insensitive Fas-induced apoptosis 4, 7 –...
Integrin-based adhesion complexes are crucial in various cellular processes, including proliferation, differentiation, and motility. While the dynamics of canonical focal (FAs) have been extensively studied, regulation physiological implications recently identified clathrin-containing (CCACs) still not well understood. In this study, we investigated spatiotemporal mechanoregulations FAs CCACs a breast cancer model. Employing single-molecule force spectroscopy coupled with live-cell...