Mechanotransduction

Mechanotransduction is the conversion of mechanical forces or material properties into biochemical signals within a cell. It lets cells sense and respond to their physical environment.

Mechanosensitive ion channel: A membrane channel that opens or closes in response to mechanical forces. Force can gate these channels, rapidly converting membrane tension into ion signals.
Cell mechanics: The study of how cells deform, generate forces, and respond to mechanical loads. Mechanotransduction is the signaling dimension of cellular mechanical behavior.
Stem cell differentiation: The process by which stem cells acquire specialized identities and functions. Matrix stiffness and applied forces can bias the cell fates stem cells adopt.
Chemotransduction: The conversion of chemical stimuli into cellular signals and responses. It contrasts sensing molecular ligands with sensing physical forces or material properties.
Integrin: A cell-surface receptor that links extracellular matrix proteins to the cytoskeleton and signaling proteins. Integrins transmit forces between the extracellular matrix and the cell interior.
Extracellular matrix: A network of proteins and carbohydrates surrounding cells in tissues. Its stiffness, composition, and organization provide mechanical cues to cells.
Durotaxis: Directed cell migration along a gradient of substrate stiffness. It shows how cells translate differences in mechanical properties into movement.
Optogenetics: A method that uses genetically encoded light-sensitive proteins to control cellular activity. Light-driven control offers an experimental counterpart to manipulating cells mechanically.
Focal adhesion: A protein assembly that connects integrins to the actin cytoskeleton and organizes cell signaling. These force-bearing junctions assemble signaling proteins where cells attach to their surroundings.
Cell membrane: A lipid bilayer that encloses a cell and regulates exchange with its surroundings. Membrane tension and curvature can directly influence force-sensitive proteins.

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