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Journal ArticleDOI

Lipid Rafts As a Membrane-Organizing Principle

Daniel Lingwood, +1 more
- 01 Jan 2010 - 
- Vol. 327, Iss: 5961, pp 46-50
TLDR
The evidence for how this principle combines the potential for sphingolipid-cholesterol self-assembly with protein specificity to selectively focus membrane bioactivity is reviewed.
Abstract
Cell membranes display a tremendous complexity of lipids and proteins designed to perform the functions cells require. To coordinate these functions, the membrane is able to laterally segregate its constituents. This capability is based on dynamic liquid-liquid immiscibility and underlies the raft concept of membrane subcompartmentalization. Lipid rafts are fluctuating nanoscale assemblies of sphingolipid, cholesterol, and proteins that can be stabilized to coalesce, forming platforms that function in membrane signaling and trafficking. Here we review the evidence for how this principle combines the potential for sphingolipid-cholesterol self-assembly with protein specificity to selectively focus membrane bioactivity.

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Hydrodynamics of soft active matter

TL;DR: This review summarizes theoretical progress in the field of active matter, placing it in the context of recent experiments, and highlights the experimental relevance of various semimicroscopic derivations of the continuum theory for describing bacterial swarms and suspensions, the cytoskeleton of living cells, and vibrated granular material.
Journal ArticleDOI

Current knowledge on exosome biogenesis and release

TL;DR: What is presently known about how exosomes are formed and released by cells is summarized and other cellular processes related to exosome biogenesis and release, such as autophagy and lysosomal exocytosis are presented.
Journal ArticleDOI

The mystery of membrane organization: composition, regulation and roles of lipid rafts

TL;DR: The membrane raft hypothesis formalized a physicochemical principle for a subtype of lateral membrane heterogeneity, in which the preferential associations between cholesterol and saturated lipids drive the formation of relatively packed membrane domains that selectively recruit certain lipids and proteins.
Journal ArticleDOI

Revitalizing membrane rafts: new tools and insights

TL;DR: How the field has matured and an evolving model in which membranes are occupied by fluctuating nanoscale assemblies of sphingolipids, cholesterol and proteins that can be stabilized into platforms that are important in signalling, viral infection and membrane trafficking are presented.
Journal ArticleDOI

Lipid metabolism in cancer

TL;DR: This review will examine some of the alterations in lipid metabolism that have been reported in cancer, at both cellular and organismal levels, and discuss how they contribute to different aspects of tumourigenesis.
References
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Journal ArticleDOI

Functional rafts in cell membranes

Kai Simons, +1 more
- 05 Jun 1997 - 
TL;DR: A new aspect of cell membrane structure is presented, based on the dynamic clustering of sphingolipids and cholesterol to form rafts that move within the fluid bilayer that function as platforms for the attachment of proteins when membranes are moved around inside the cell and during signal transduction.
Journal ArticleDOI

The fluid mosaic model of the structure of cell membranes.

TL;DR: Results strongly indicate that the bivalent antibodies produce an aggregation of the surface immunoglobulin molecules in the plane of the membrane, which can occur only if the immunoglOBulin molecules are free to diffuse in the membrane.
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 ArticleDOI

High-Resolution Crystal Structure of an Engineered Human β2-Adrenergic G Protein–Coupled Receptor

TL;DR: Although the location of carazolol in the β2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopin as a template model for this large receptor family.
Journal ArticleDOI

Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface

TL;DR: It is shown that a protein with a glycosylphosphatidyl inositol (GPI) anchor can be recovered from lysates of epithelial cells in a low density, detergent-insoluble form, supporting the model proposed by Simons and colleagues for sorting of certain membrane proteins to the apical surface after intracellular association with glycosphingolipids.
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