Stossel T P
Philos Trans R Soc Lond B Biol Sci. 1982 Nov 4;299(1095):275-89. doi: 10.1098/rstb.1982.0132.
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.
吞噬性白细胞富含肌动蛋白的皮质细胞质形成伪足,并通过产生定向推进力和收缩力来控制细胞形状和运动。从白细胞中纯化的蛋白质形成并使肌动蛋白基质变形。肌动蛋白结合蛋白(ABP)将肌动蛋白丝交联成具有垂直分支的三维晶格。这种结构可以在电子显微镜下观察到,与肌动蛋白-ABP基质的物理特性一致。凝溶胶蛋白在有钙的情况下以高亲和力结合肌动蛋白丝的一端;另一种蛋白质尖形蛋白则以低亲和力持续结合另一端。这些蛋白质共同作用可以控制肌动蛋白丝的长度,从而调节肌动蛋白网络的扩张(推进)或收缩。网络的组装状态也控制基于肌球蛋白的收缩力。一场拔河比赛决定了晶格运动的方向,结构较少的区域倾向于向结构较多的区域移动。