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 是运输 III (ESCRT-III) 超家族所需的内体分选复合体的成员，其成员形成多种基于丝的超分子结构，促进膜变形和裂变。溶液中的 VIPP1 冷冻电子显微镜 (EM) 结构显示螺旋杆和堆叠环篮，管腔中具有两亲性膜结合域。然而，VIPP1 如何与膜相互作用仍然很大程度上未知。在这里，我们使用高速原子力显微镜 (HS-AFM) 表明，VIPP1 通过类似 ESCRT-III 的细丝组装和动力学，在支持的脂质双层上组装成右手手性螺旋和正多边形。 VIPP1细丝通过在环形中心聚合中心的聚合顺时针生长成螺旋，并通过在扇区外围的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线，成熟后通过将股线横向退火到外部低曲率螺线转而转变为对数螺线。