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Item does not contain fulltext, 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.

With the coming of age of virtual/augmented reality and interactive media, numerous definitions, frameworks, and models of immersion have emerged across different fields ranging from computer graphics to literary works. Immersion is oftentimes used interchangeably with presence as both concepts are closely related. However, there are noticeable interdisciplinary differences regarding definitions, scope, and constituents that are required to be addressed so that a coherent understanding of the concepts can be achieved. Such consensus is vital for paving the directionality of the future of immersive media experiences (IMEx) and all related matters. The aim of this white paper is to provide a survey of definitions of immersion and presence which leads to a definition of immersive media experience (IMEx). The Quality of Experience (QoE) for immersive media is described by establishing a relationship between the concepts of QoE and IMEx followed by application areas of immersive media experience. Influencing factors on immersive media experience are elaborated as well as the assessment of immersive media experience. Finally, standardization activities related to IMEx are highlighted and the white paper is concluded with an outlook related to future developments.

Contains fulltext : 172064.pdf (publisher's version ) (Open Access), Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P-2) is a minor component of total plasma membrane lipids, but it has a substantial role in the regulation of many cellular functions, including exo- and endocytosis. Recently, it was shown that PI(4,5)P-2 and syntaxin 1, a SNARE protein that catalyzes regulated exocytosis, form domains in the plasma membrane that constitute recognition sites for vesicle docking. Also, calcium was shown to promote syntaxin 1 clustering in the plasma membrane, but the molecular mechanism was unknown. Here, using a combination of superresolution stimulated emission depletion microscopy, FRET, and atomic force microscopy, we show that Ca2+ acts as a charge bridge that specifically and reversibly connects multiple syntaxin 1/PI(4,5)P-2 complexes into larger mesoscale domains. This transient reorganization of the plasma membrane by physiological Ca2+ concentrations is likely to be important for Ca2+-regulated secretion.

Contains fulltext : 153020.pdf (publisher's version ) (Open Access), The clustering of proteins and lipids in distinct microdomains is emerging as an important principle for the spatial patterning of biological membranes. Such domain formation can be the result of hydrophobic and ionic interactions with membrane lipids as well as of specific protein-protein interactions. Here using plasma membrane-resident SNARE proteins as model, we show that hydrophobic mismatch between the length of transmembrane domains (TMDs) and the thickness of the lipid membrane suffices to induce clustering of proteins. Even when the TMDs differ in length by only a single residue, hydrophobic mismatch can segregate structurally closely homologous membrane proteins in distinct membrane domains. Domain formation is further fine-tuned by interactions with polyanionic phosphoinositides and homo and heterotypic protein interactions. Our findings demonstrate that hydrophobic mismatch contributes to the structural organization of membranes.