The structure of cortical cytoplasm.
Actin-rich cortical cytoplasm of phagocytic leucocytes forms pseudopodia and controls cell shape and movement by generating directional propulsive and contractile forces. Proteins purified from leucocytes form and deform an actin matrix. Actin-binding protein (ABP) cross-links actin filaments into a three-dimensional lattice with perpendicular branches. This structure, which can be visualized in the electron microscope, is consistent with physical properties of actin-ABP matrices. Gelsolin binds one end of actin filaments with high affinity in the presence of calcium; acumentin, another protein, constitutively binds the other end with low affinity. Together these proteins can control actin filament length and thereby regulate expansion (propulsion) or collapse of the actin network. The assembly state of the network also controls myosin-based contractile forces. A tug-of-war decides the direction of lattice movement, regions of lesser structure tending to move toward regions of greater structure.
D000199:Actins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism; D003593:Cytoplasm / Q000648:ultrastructure; D003599:Cytoskeleton / Q000648:ultrastructure*; D018260:Gelsolin; D006801:Humans; D007962:Leukocytes / Q000648:ultrastructure*; D008840:Microfilament Proteins; D008854:Microscopy, Electron; D014783:Viscosity
D000199:Actins; D002352:Carrier Proteins; D018260:Gelsolin; D008840:Microfilament Proteins; C016953:brevin