Dataset of ESCRT-III polymer rings (CdvB, CdvB1 and CdvB2) in wildtype archaea (Sacidocaldarius_DSM639) imaged by (dyMIN) STED nanoscopy.

Dataset of ESCRT-III polymer rings (CdvB, CdvB1 and CdvB2) in wildtype archaea (Sacidocaldarius_DSM639) imaged by (dyMIN) STED nanoscopy. The dataset contains the raw STED image files (16bit .tiff format) on which the analysis was performed to determine the relative positions between CdvB, CdvB1 and CdvB2. Additionally, it contains raw STED images of CdvB1 and CdvB2 in wildtype Sacidocaldarius DSM639 with a constricting neck. The data with constricting necks was subdivided in a category with and without the presence of CdvB

Giant worm-shaped ESCRT scaffolds surround actin-independent integrin clusters.

Endosomal Sorting Complex Required for Transport (ESCRT) proteins can be transiently recruited to the plasma membrane for membrane repair and formation of extracellular vesicles. Here, we discovered micrometer-sized worm-shaped ESCRT structures that stably persist for multiple hours at the plasma membrane of macrophages, dendritic cells, and fibroblasts. These structures surround clusters of integrins and known cargoes of extracellular vesicles. The ESCRT structures are tightly connected to the cellular support and are left behind by the cells together with surrounding patches of membrane. The phospholipid composition is altered at the position of the ESCRT structures, and the actin cytoskeleton is locally degraded, which are hallmarks of membrane damage and extracellular vesicle formation. Disruption of actin polymerization increased the formation of the ESCRT structures and cell adhesion. The ESCRT structures were also present at plasma membrane contact sites with membrane-disrupting silica crystals. We propose that the ESCRT proteins are recruited to adhesion-induced membrane tears to induce extracellular shedding of the damaged membrane