Journal ArticleDOI
The distribution and function of phosphatidylserine in cellular membranes.
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TLDR
The determinants and functional implications of the subcellular distribution and membrane topology of the most abundant negatively charged phospholipid in eukaryotic membranes are discussed.Abstract:
Phosphatidylserine (PS) is the most abundant negatively charged phospholipid in eukaryotic membranes. PS directs the binding of proteins that bear C2 or gamma-carboxyglutamic domains and contributes to the electrostatic association of polycationic ligands with cellular membranes. Rather than being evenly distributed, PS is found preferentially in the inner leaflet of the plasma membrane and in endocytic membranes. The loss of PS asymmetry is an early indicator of apoptosis and serves as a signal to initiate blood clotting. This review discusses the determinants and functional implications of the subcellular distribution and membrane topology of PS.read more
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Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores
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Journal ArticleDOI
Calcium-dependent phospholipid scrambling by TMEM16F
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Journal ArticleDOI
Piezo proteins are pore-forming subunits of mechanically activated channels
Bertrand Coste,Bailong Xiao,Jose S. Santos,Ruhma Syeda,Jörg Grandl,Jörg Grandl,Kathryn S. R. Spencer,Sung-Eun Kim,Manuela Schmidt,Jayanti Mathur,Adrienne E. Dubin,Mauricio Montal,Ardem Patapoutian,Ardem Patapoutian +13 more
TL;DR: It is shown that Drosophila melanogaster Piezo (DmPiezo, also called CG8486) also induces mechanically activated currents in cells, but through channels with remarkably distinct pore properties including sensitivity to the pore blocker ruthenium red and single channel conductances, demonstrating that Piezo proteins are an evolutionarily conserved ion channel family involved in mechanotransduction.
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Lipid Map of the Mammalian Cell
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References
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Journal ArticleDOI
Membrane lipids: where they are and how they behave.
TL;DR: How do cells apply anabolic and catabolic enzymes, translocases and transporters, plus the intrinsic physical phase behaviour of lipids and their interactions with membrane proteins, to create the unique compositions and multiple functions of their individual membranes?
Journal Article
Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages.
Valerie A. Fadok,Dennis R. Voelker,Priscilla A. Campbell,J. John Cohen,D L Bratton,Peter M. Henson +5 more
TL;DR: The data suggest that macrophages specifically recognize phosphatidylserine that is exposed on the surface of lymphocytes during the development of apoptosis, and suggest that apoptotic lymphocytes lose membrane phospholipid asymmetry and expose phosphorus on the outer leaflet of the plasma membrane.
Journal ArticleDOI
Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl.
Seamus J. Martin,Chris P. M. Reutelingsperger,A J McGahon,J. A. Rader,R. C. A. A. Van Schie,Drake LaFace,Douglas R. Green +6 more
TL;DR: It is shown that PS externalization is an early and widespread event during apoptosis of a variety of murine and human cell types, regardless of the initiating stimulus, and precedes several other events normally associated with this mode of cell death.
Journal ArticleDOI
Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis.
Gerrit Koopman,Chris P. M. Reutelingsperger,G. A. M. Kuijten,R. M. J. Keehnen,Steven T. Pals,M. H. J. Van Oers +5 more
TL;DR: The results indicate that the phase in apoptosis that is characterized by chromatin condensation coincides with phosphatidylserine exposure, which precedes membrane damage that might lead to release from the cells of enzymes that are harmful to the surrounding tissues.
Journal ArticleDOI
Membrane recognition by phospholipid-binding domains.
TL;DR: Many different globular domains bind to the surfaces of cellular membranes, or to specific phospholipid components in these membranes, and this binding is often tightly regulated.