1. Giant worm-shaped ESCRT scaffolds surround actin-independent integrin clusters.
- Author
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Stempels FC, Jiang M, Warner HM, Moser ML, Janssens MH, Maassen S, Nelen IH, de Boer R, Jiemy WF, Knight D, Selley J, O'Cualain R, Baranov MV, Burgers TCQ, Sansevrino R, Milovanovic D, Heeringa P, Jones MC, Vlijm R, Ter Beest M, and van den Bogaart G
- Subjects
- Protein Transport, Phospholipids chemistry, Cell Membrane, Macrophages, Dendritic Cells, Fibroblasts, Humans, Protein Conformation, Actins metabolism, Endosomal Sorting Complexes Required for Transport genetics, Endosomal Sorting Complexes Required for Transport metabolism, Integrins genetics, Integrins metabolism
- Abstract
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., (© 2023 Stempels et al.)
- Published
- 2023
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