The biogenesis and maintenance of thylakoid membranes require vesicle-inducing protein in plastids 1 (VIPP1). VIPP1 is a member of the endosomal sorting complex required for transport-III (ESCRT-III) superfamily, whose members form diverse filament-based supramolecular structures that facilitate membrane deformation and fission. VIPP1 cryo-electron microscopy (EM) structures in solution revealed helical rods and baskets of stacked rings, with amphipathic membrane-binding domains in the lumen. However, how VIPP1 interacts with membranes remains largely unknown. Here, using high-speed atomic force microscopy (HS-AFM), we show that VIPP1 assembles into right-handed chiral spirals and regular polygons on supported lipid bilayers via ESCRT-III-like filament assembly and dynamics. VIPP1 filaments grow clockwise into spirals through polymerization at a ring-shaped central polymerization hub, and into polygons through clockwise polymerization at the sector peripheries. Interestingly, VIPP1 initially forms Archimedean spirals, which upon maturation transform into logarithmic spirals through lateral annealing of strands to the outermore low-curvature spiral turns.

类囊体膜的生物发生和维持需要质体中的囊泡诱导蛋白 1 （VIPP1）。VIPP1 是 transport-III （ESCRT-III） 超家族所需的内体分选复合物的成员，其成员形成多种基于细丝的超分子结构，可促进膜变形和裂变。溶液中的 VIPP1 冷冻电子显微镜 （EM） 结构显示螺旋杆和篮子堆叠环，管腔中具有两亲性膜结合结构域。然而，VIPP1 如何与膜相互作用在很大程度上仍然未知。在这里，使用高速原子力显微镜 （HS-AFM），我们表明 VIPP1 通过类似 ESCRT-III 的细丝组装和动力学在支撑的脂质双层上组装成右手性螺旋和规则多边形。VIPP1 细丝在环形中央聚合中心通过聚合顺时针生长成螺旋，在扇区外围通过顺时针聚合生长成多边形。有趣的是，VIPP1 最初形成阿基米德螺旋，成熟后通过股束横向退火到更外侧的低曲率螺旋转向，转变为对数螺旋。