动物和真菌细胞的细胞分裂主要取决于Anillin支架蛋白。裂变酵母Anillin相关的Mid1将细胞动力学环前体节点锚定到膜上。然而,尚不清楚其Pleckstrin同源性(PH)和C2C末端结构域是否都作为单体或二聚体与膜结合,如果一个领域起主导作用。我们研究了具有酵母样脂质组成的膜附近的Mid1膜与全原子分子动力学的结合。在全C末端区域开始远离膜的模拟中,Mid1以垂直方向通过C2的无序L3环结合,PH远离膜。然而,具有最初与膜结合的C2和PH两者的构型保持与膜相关联。C2-PH二聚体的模拟显示广泛的不对称膜接触。这些多种结合模式可能反映了Mid1与膜的多种相互作用,节点蛋白,以及承受机械力的能力.
Cytokinesis of animal and fungi cells depends crucially on the anillin scaffold proteins. Fission yeast anillin-related Mid1 anchors cytokinetic ring precursor nodes to the membrane. However, it is unclear if both of its Pleckstrin Homology (PH) and C2 C-terminal domains bind to the membrane as monomers or dimers, and if one domain plays a dominant role. We studied Mid1 membrane binding with all-atom molecular dynamics near a membrane with yeast-like lipid composition. In simulations with the full C terminal region started away from the membrane, Mid1 binds through the disordered L3 loop of C2 in a vertical orientation, with the PH away from the membrane. However, a configuration with both C2 and PH initially bound to the membrane remains associated with the membrane. Simulations of C2-PH dimers show extensive asymmetric membrane contacts. These multiple modes of binding may reflect Mid1\'s multiple interactions with membranes, node proteins, and ability to sustain mechanical forces.