Biochemistry Department, University of Geneva, 1211 Geneva, Switzerland.
Cell. 2012 Oct 26;151(3):619-29. doi: 10.1016/j.cell.2012.09.017.
The GTPase dynamin polymerizes into a helical coat that constricts membrane necks of endocytic pits to promote their fission. However, the dynamin mechanism is still debated because constriction is necessary but not sufficient for fission. Here, we show that fission occurs at the interface between the dynamin coat and the uncoated membrane. At this location, the considerable change in membrane curvature increases the local membrane elastic energy, reducing the energy barrier for fission. Fission kinetics depends on tension, bending rigidity, and the dynamin constriction torque. Indeed, we experimentally find that the fission rate depends on membrane tension in vitro and during endocytosis in vivo. By estimating the energy barrier from the increased elastic energy at the edge of dynamin and measuring the dynamin torque, we show that the mechanical energy spent on dynamin constriction can reduce the energy barrier for fission sufficiently to promote spontaneous fission. :
GTPase 动力蛋白聚合成一个螺旋状的外壳,压缩内吞陷窝的膜颈部,促进它们的分裂。然而,动力蛋白的机制仍存在争议,因为收缩对于分裂是必要的,但不是充分的。在这里,我们表明分裂发生在动力蛋白外壳和未包被的膜之间的界面处。在这个位置,膜曲率的显著变化会增加局部膜弹性能量,从而降低分裂的能量势垒。分裂动力学取决于张力、弯曲刚度和动力蛋白的收缩扭矩。事实上,我们在实验中发现,分裂速率取决于体外的膜张力和体内的内吞作用。通过估计在动力蛋白边缘增加的弹性能量来计算能量势垒,并测量动力蛋白的扭矩,我们表明,动力蛋白收缩所消耗的机械能可以降低分裂的能量势垒,足以促进自发分裂。