Cited by 9,757Lipid Membrane Structure and BehaviorCaveolin-1 and cellular processesSphingolipid Metabolism and Signaling

The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.

Functional rafts in cell membranes

Simons, Kai, Ikonen, Elina·1997·Nature

DOI 10.1038/42408

Open this paper in CoChat — free account

Abstract

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. It is proposed that these rafts function as platforms for the attachment of proteins when membranes are moved around inside the cell and during signal transduction.

Integrity signals

Registry

Crossref · 10.1038/42408

Cites

68 of 68 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

The Fluid Mosaic Model of the Structure of Cell Membranes
Singer, S. J., & Nicolson, G. L. (1972) · Science · doi:10.1126/science.175.4023.720 · Cited by 9,158
Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
Brown, D. A., & Rose, J. K. (1992) · Cell · doi:10.1016/0092-8674(92)90189-j · Cited by 2,921
Lipid sorting in epithelial cells
Simons, K., & Gerrit van, M. E. E. R. (1988) · Biochemistry · doi:10.1021/bi00417a001 · Cited by 1,373
Self-citation
Protein Sorting by Transport Vesicles
Rothman, J. E., & Wieland, F. (1996) · Science · doi:10.1126/science.272.5259.227 · Cited by 1,156
Morphogenesis of the Polarized Epithelial Cell Phenotype
Rodriguez-Boulan, E. J., & Nelson, W. J. (1989) · Science · doi:10.1126/science.2672330 · Cited by 1,085
Co-purification and Direct Interaction of Ras with Caveolin, an Integral Membrane Protein of Caveolae Microdomains
Song, K. S., Li, S. C., Okamoto, T., Quilliam, L. A., Sargiacomo, M., & Lisanti, M. P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9690 · Cited by 1,000
Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
Sargiacomo, M., Sudol, M., Tang, Z., & Lisanti, M. P. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.122.4.789 · Cited by 947
Filipin-sensitive caveolae-mediated transport in endothelium: reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules.
Schnitzer, J. E., Oh, P., Pinney, E., & Allard, J. F. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.127.5.1217 · Cited by 928
VIP21/caveolin is a cholesterol-binding protein.
Murata, M., Peränen, J., Schreiner, R., Wieland, F., Kurzchalia, T. V., & Simons, K. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.22.10339 · Cited by 899
Self-citation
MDR1 P-Glycoprotein Is a Lipid Translocase of Broad Specificity, While MDR3 P-Glycoprotein Specifically Translocates Phosphatidylcholine
van Helvoort, A., Smith, A. J., Sprong, H., Fritzsche, I., Schinkel, A. H., Borst, P., & Gerrit van, M. E. E. R. (1996) · Cell · doi:10.1016/s0092-8674(00)81370-7 · Cited by 854

Flagged first, then by citations

Show all 68 references

Sorted by citations

Items 401–500 of 1,044

Lipid Rafts and the Regulation of Exocytosis
Salaün, C., James, D. J., & Chamberlain, L. H. (2004) · Traffic · doi:10.1111/j.1600-0854.2004.0162.x · Cited by 301
Vesicular and non-vesicular sterol transport in living cells
Hao, M., Lin, S. X., Karylowski, O. J., Wüstner, D., McGraw, T. E., & Maxfield, F. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108861200 · Cited by 285
Caveolin-1 and -2 in the Exocytic Pathway of MDCK Cells
Scheiffele, P., Verkade, P., Fra, A., Virta, H., Simons, K., & Ikonen, E. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.4.795 · Cited by 301
Self-citation
HDL in innate and adaptive immunity
Catapano, A. L., Pirillo, A., Bonacina, F., & Norata, G. D. (2014) · Cardiovascular Research · doi:10.1093/cvr/cvu150 · Cited by 301
Membrane Elasticity in Giant Vesicles with Fluid Phase Coexistence
Baumgart, T., Das, S. L., Webb, W. W., & Jenkins, J. T. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.049692 · Cited by 300
Glycosphingolipids: synthesis and functions
D’Angelo, G., Capasso, S., Sticco, L., & Russo, D. (2013) · FEBS Journal · doi:10.1111/febs.12559 · Cited by 297
GM3-enriched Microdomain Involved in Cell Adhesion and Signal Transduction through Carbohydrate-Carbohydrate Interaction in Mouse Melanoma B16 Cells
Iwabuchi, K., Yamamura, S., Prinetti, A., Handa, K., & Hakomori, S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.15.9130 · Cited by 299
Lipid Rafts have Different Sizes Depending on Membrane Composition: A Time-resolved Fluorescence Resonance Energy Transfer Study
de Almeida, R. F. M., Loura, L. M. S., Fedorov, A., & PRIETO, M. J. E. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.12.026 · Cited by 298
Molecular basis of the functionalpodocin-nephrin complex: mutations in the NPHS2 gene disrupt nephrin targeting to lipid raft microdomains
Huber, T. B. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg360 · Cited by 297
Role of cholesterol in the function and organization of G-protein coupled receptors
Pucadyil, T. J., & Chattopadhyay, A. (2006) · Progress in Lipid Research · doi:10.1016/j.plipres.2006.02.002 · Cited by 300
Plasma membrane microdomains
Maxfield, F. R. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00351-4 · Cited by 296
Drosophila Dpp Morphogen Movement Is Independent of Dynamin-Mediated Endocytosis but Regulated by the Glypican Members of Heparan Sulfate Proteoglycans
Belenkaya, T. Y., Han, C., Yan, D., Opoka, R. J., Khodoun, M. V., Liu, H., & Lin, X. (2004) · Cell · doi:10.1016/j.cell.2004.09.031 · Cited by 296
Compartmentalized signaling by GPI-anchored ephrin-A5 requires the Fyn tyrosine kinase to regulate cellular adhesionPreprint
Davy, A., Gale, N. W., Murray, E. W., Klinghoffer, R. A., Soriano, P. M., Feuerstein, C., & Robbins, S. M. (1999) · Genes & Development · doi:10.1101/gad.13.23.3125 · Cited by 296
Feeding Our Immune System: Impact on Metabolism
Wolowczuk, I., Verwaerde, C., Viltart, O., Delanoye, A., Delacre, M., Pot, B., & Grangette, C. (2008) · Clinical and Developmental Immunology · doi:10.1155/2008/639803 · Cited by 307
“Moreover, lipids are major components of cell membranes, and combinational associations of different lipid species will generate microheterogeneity in cell membranes, leading to the formation of microdomains, termed rafts [91, 92].”
Background
New insights in glycosphingolipid function: "glycosignaling domain," a cell surface assembly of glycosphingolipids with signal transducer molecules, involved in cell adhesion coupled with signaling
Hakomori, S., Handa, K., Iwabuchi, K., Yamamura, S., & Prinetti, A. (1998) · Glycobiology · doi:10.1093/oxfordjournals.glycob.a018822 · Cited by 295
Assessing the Nature of Lipid Raft Membranes
Niemelä, P. S., Ollila, O. H. S., Hyvönen, M., Karttunen, M., & Vattulainen, I. (2007) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0030034 · Cited by 294
Intracellular cholesterol transport
Maxfield, F. R., & Wüstner, D. (2002) · Journal of Clinical Investigation · doi:10.1172/jci16500 · Cited by 305
Assembly of Myelin by Association of Proteolipid Protein with Cholesterol- and Galactosylceramide-Rich Membrane Domains
Simons, M., Krämer, E.-M., Thiele, C., Stoffel, W., & Trotter, J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.1.143 · Cited by 293
Lessons of Slicing Membranes: Interplay of Packing, Free Area, and Lateral Diffusion in Phospholipid/Cholesterol Bilayers
Falck, E., Patra, M., Karttunen, M., Hyvönen, M., & Vattulainen, I. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.041368 · Cited by 293
Brain Membrane Phospholipid Alterations in Alzheimer's Disease
Pettegrew, J. W., Panchalingam, K., Hamilton, R. L., & McClure, R. J. (2001) · Neurochemical Research · doi:10.1023/a:1011603916962 · Cited by 292
Polyunsaturated fatty acid–cholesterol interactions: Domain formation in membranes
Wassall, S. R., & Stillwell, W. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.10.011 · Cited by 292
Lipid Profiling by Multiple Precursor and Neutral Loss Scanning Driven by the Data-Dependent Acquisition
Schwudke, D., Oegema, J., Burton, L., Entchev, E. V., Hannich, J. T., Ejsing, C. S., Kurzchalia, T. V., & Shevchenko, A. (2005) · Analytical Chemistry · doi:10.1021/ac051605m · Cited by 292
Dynasore - not just a dynamin inhibitor
Preta, G., Cronin, J., & Sheldon, I. M. (2015) · Cell Communication and Signaling · doi:10.1186/s12964-015-0102-1 · Cited by 292
“Lipid rafts are membrane microdomains that are enriched in cholesterol, sphingomyelin, sphingolipids and phospholipids, and these areas of membrane differ in composition from the surrounding regions of plasma membrane [41,42].”
Evaluation of Prototype Transmembrane 4 Superfamily Protein Complexes and Their Relation to Lipid Rafts
Claas, C., Stipp, C. S., & Hemler, M. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008650200 · Cited by 292
Sorting of Lipids and Proteins in Membrane Curvature Gradients
Tian, A., & Baumgart, T. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.11.067 · Cited by 294
“The biological relevance of phase partitioning associated with fluid phase coexistence is currently a matter of intense biophysical interest (43,44).”
Background
Intracellular cholesterol transport
Fielding, C. J., & Fielding, P. E. (1997) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)37169-8 · Cited by 291
The sterol-sensing domain: multiple families, a unique role?
Kuwabara, P. E., & Labouesse, M. (2002) · Trends in Genetics · doi:10.1016/s0168-9525(02)02640-9 · Cited by 285
Ceramide‐rich platforms in transmembrane signaling
Stancevic, B., & Kolesnick, R. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.026 · Cited by 291
Released GFRα1 Potentiates Downstream Signaling, Neuronal Survival, and Differentiation via a Novel Mechanism of Recruitment of c-Ret to Lipid Rafts
Paratcha, G., Ledda, F., Baars, L., Coulpier, M., Besset, V., Anders, J., Scott, R. P., & Ibáñez, C. F. (2001) · Neuron · doi:10.1016/s0896-6273(01)00188-x · Cited by 290
Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance
Enkavi, G., Javanainen, M., Kulig, W., Róg, T., & Vattulainen, I. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00538 · Cited by 293
Cosignaling of NCAM via lipid rafts and the FGF receptor is required for neuritogenesis
Niethammer, P., Delling, M., Sytnyk, V., Dityatev, A. E., Fukami, K., & Schachner, M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200109059 · Cited by 294
Cytoskeletal polarization and redistribution of cell-surface molecules during T cell antigen recognition
van der Merwe, P. A., Davis, S. J., Shaw, A. S., & Dustin, M. L. (2000) · Seminars in Immunology · doi:10.1006/smim.2000.0203 · Cited by 290
The anti‐amnesic and neuroprotective effects of donepezil against amyloid β25‐35peptide‐induced toxicity in mice involve an interaction with theσ1receptor
Meunier, J., Ieni, J. R., & Maurice, T. (2006) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706927 · Cited by 294
Membrane anchored serine proteases: A rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer
Netzel–Arnett, S., Hooper, J. D., Szabo, R., Madison, E. L., Quigley, J. P., Bugge, T. H., & Antalis, T. (2003) · Cancer and Metastasis Reviews · doi:10.1023/a:1023003616848 · Cited by 289
Lipids as Modulators of Proteolytic Activity of BACE
Kalvodova, L., Kahya, N., Schwille, P., Ehehalt, R., Verkade, P., Drechsel, D. N., & Simons, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504484200 · Cited by 297
Self-citation
Biophysics of cell membrane lipids in cancer drug resistance: Implications for drug transport and drug delivery with nanoparticles
Peetla, C., Vijayaraghavalu, S., & Labhasetwar, V. D. (2013) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2013.09.004 · Cited by 300
“Lipid rafts exist in the liquid-ordered phase state and are rich in cholesterol and sphingolipids [81].”
Background
Cholesterol depletion induces large scale domain segregation in living cell membranes
Hao, M., Mukherjee, S., & Maxfield, F. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.231377398 · Cited by 289
The mechanism of internalization of glycosylphosphatidylinositol‐anchored prion protein
Sunyach, C., Jen, A., Deng, J., Fitzgerald, K. T., Frobert, Y., Grassi, J. J., McCaffrey, M., & Morris, R. J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg344 · Cited by 288
Cyclic β-1,2-glucan is a brucella virulence factor required for intracellular survival
Arellano-Reynoso, B., Lapaque, N., Salcedo, S. P., Briones, G., Ciocchini, A. E., Ugalde, R. A., Moreno, E., Moriyón, I., & Gorvel, J. (2005) · Nature Immunology · doi:10.1038/ni1202 · Cited by 288
Cholesterol Rules
de la Serna, J. B., Pérez‐Gil, J., Simonsen, A. C., & Bagatolli, L. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404648200 · Cited by 285
Structural determinants and functional consequences of protein affinity for membrane rafts
Lorent, J. H., Diaz-Rohrer, B. B., Lin, X., Spring, K., Gorfe, A. A., Levental, K. R., & Levental, I. (2017) · Nature Communications · doi:10.1038/s41467-017-01328-3 · Cited by 285
Visualization of Protein Compartmentation within the Plasma Membrane of Living Yeast Cells
Malínská, K., Malínský, J., Opekarová, M., & Tanner, W. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-04-0221 · Cited by 283
Sphingolipids in mammalian cell signalling
Ohanian, J., & Ohanian, V. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000836 · Cited by 283
Human Immunodeficiency Virus Type 1 Enters Brain Microvascular Endothelia by Macropinocytosis Dependent on Lipid Rafts and the Mitogen-Activated Protein Kinase Signaling Pathway
Liu, N. Q., Lossinsky, A. S., Popik, W., Li, X., Gujuluva, C. N., Kriederman, B., Roberts, J., Pushkarsky, T., Bukrinsky, M., Witte, M. H., et al. (2002) · Journal of Virology · doi:10.1128/jvi.76.13.6689-6700.2002 · Cited by 282
IgA and the IgA Fc receptor
van Egmond, M., Damen, C. A., van Spriel, A. B., Vidarsson, G., van Garderen, E., & van de Winkel, J. G. J. (2001) · Trends in Immunology · doi:10.1016/s1471-4906(01)01873-7 · Cited by 282
Insect Sterol Nutrition and Physiology: A Global Overview
Behmer, S. T., & Nes, W. D. (2003) · Advances in insect physiology · doi:10.1016/s0065-2806(03)31001-x · Cited by 281
Biochemical Interactions Integrating Itk with the T Cell Receptor-initiated Signaling Cascade
Bunnell, S. C., Diehn, M., Yaffe, M. B., Findell, P. R., Cantley, L. C., & Berg, L. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.3.2219 · Cited by 283
Mammalian Sprouty-1 and -2 Are Membrane-Anchored Phosphoprotein Inhibitors of Growth Factor Signaling in Endothelial Cells
Impagnatiello, M.-A., Weitzer, S., Gannon, G., Compagni, A., Cotten, M. L., & Christofori, G. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.5.1087 · Cited by 279
Rab proteins: The key regulators of intracellular vesicle transport
Bhuin, T., & Roy, J. K. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.07.027 · Cited by 301
“The dynamic properties of a Rab5 domain probably include a spatial and temporal control over PtdIns (3) P synthesis and turnover [71,72,10].”
Background
Lipid rafts as signaling hubs in cancer cell survival/death and invasion: implications in tumor progression and therapy
Mollinedo, F., & Gajate, C. (2020) · Journal of Lipid Research · doi:10.1194/jlr.tr119000439 · Cited by 297
“In addition to the above processes, cholesterol is a major regulator of lipid organization, being responsible for the close packing of acyl chains of phospholipids, promoting phase separation, and stabilizing the formation of cholesterol- and sphingolipid-rich membrane microdomains known as lipid rafts or membrane raf…”
Background
Lipid rafts and HIV-1: from viral entry to assembly of progeny virions
Campbell, S. M., Crowe, S. M., & Mak, J. (2001) · Journal of Clinical Virology · doi:10.1016/s1386-6532(01)00193-7 · Cited by 280
Electrospray ionization tandem mass spectrometry of glycerophosphoethanolamine plasmalogen phospholipids
Berry, K. A. Z., & Murphy, R. C. (2004) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2004.07.009 · Cited by 279
Molecular View of Cholesterol Flip-Flop and Chemical Potential in Different Membrane Environments
Bennett, W. F., MacCallum, J. L., Hinner, M. J., Marrink, ‪. J., & Tieleman, D. P. (2009) · Journal of the American Chemical Society · doi:10.1021/ja903529f · Cited by 286
Targeting of Shiga Toxin B-Subunit to Retrograde Transport Route in Association with Detergent-resistant Membranes
Falguières, T., Mallard, F., Baron, C. L., Hanau, D., Lingwood, C. A., Goud, B., Salamero, J., & Johannes, L. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2453 · Cited by 279
Protein Crowding in Lipid Bilayers Gives Rise to Non-Gaussian Anomalous Lateral Diffusion of Phospholipids and Proteins
Jeon, J., Javanainen, M., Martinez‐Seara, H., Metzler, R., & Vattulainen, I. (2016) · Physical Review X · doi:10.1103/physrevx.6.021006 · Cited by 277
“fluids characterized by heterogeneity [6,8] and compart-”
The Ca2+-dependent protein kinase CPK3 is required for MAPK-independent salt-stress acclimation in Arabidopsis
Mehlmer, N., Wurzinger, B., Stael, S., Hofmann-Rodrigues, D., Csaszar, E., Pfister, B., Bayer, R. G., & Teige, M. (2010) · The Plant Journal · doi:10.1111/j.1365-313x.2010.04257.x · Cited by 278
“…as lipid rafts – cause a spatial organization of protein complexes with important functions in signalling was developed for animal cells years ago (Simons and Ikonen, 1997; Simons and Toomre, 2000), but only recently has evidence for this phenomenon been obtained for plant cells (Morel et al. ,…”
Domains and Rafts in Lipid Membranes
Binder, W. H., Barragan‐Montero, V., & Menger, F. M. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200300586 · Cited by 285
Detergent resistance as a tool in membrane research
Lingwood, D., & Simons, K. (2007) · Nature Protocols · doi:10.1038/nprot.2007.294 · Cited by 276
“In combination with tight cholesterol interdigitation, this results in a more condensed assemblage in a phase that is separate from the surrounding liquid-disordered unsaturated glycerophospholipid”
BackgroundSelf-citation
Langmuir monolayers as models to study processes at membrane surfaces
Stefaniu, C., Brezesinski, G., & Möhwald, H. (2014) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2014.02.013 · Cited by 281
“In the early 70's it was already concluded from electron spin resonance and electron microscopic studies, that there are domains of ordered phases in a lake of disordered phase of bilayers [39], and these domains later became popular as ‘rafts’ [40,41].”
Background
Intracellular cholesterol transport
Maxfield, F. R., & Wüstner, D. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216500 · Cited by 273
Structure and function of glycosphingolipids and sphingolipids: Recollections and future trends
Hakomori, S. (2007) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2007.08.015 · Cited by 283
Simulation Studies of Protein-Induced Bilayer Deformations, and Lipid-Induced Protein Tilting, on a Mesoscopic Model for Lipid Bilayers with Embedded Proteins
Venturoli, M., Smit, B., & Sperotto, M. M. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.050849 · Cited by 274
The Nef protein of HIV-1 associates with rafts and primes T cells for activation
Wang, J.-K., Kiyokawa, E., Verdin, E. M., & Trono, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.1.394 · Cited by 282
Measles Viruses with Altered Envelope Protein Cytoplasmic Tails Gain Cell Fusion Competence
Cathomen, T., Naim, H. Y., & Cattaneo, R. (1998) · Journal of Virology · doi:10.1128/jvi.72.2.1224-1234.1998 · Cited by 273
Integrin-mediated adhesion regulates membrane order
Gaus, K., Lay, S. L., Balasubramanian, N., & Schwartz, M. A. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200603034 · Cited by 272
Targeted cytoplasmic irradiation induces bystander responses
Shao, C., Folkard, M., Michael, B. D., & Prise, K. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404930101 · Cited by 272
Ceramide-mediated clustering is required for CD95-DISC formation
Grassmé, H., Cremesti, A. E., Kolesnick, R., & Gulbins, E. (2003) · Oncogene · doi:10.1038/sj.onc.1206540 · Cited by 271
The Structural Role of Cholesterol in Cell Membranes: From Condensed Bilayers to Lipid Rafts
Krause, M. R., & Regen, S. L. (2014) · Accounts of Chemical Research · doi:10.1021/ar500260t · Cited by 288
Molecular Targets of Epigallocatechin—Gallate (EGCG): A Special Focus on Signal Transduction and Cancer
Negri, A., Naponelli, V., Rizzi, F., & Bettuzzi, S. (2018) · Nutrients · doi:10.3390/nu10121936 · Cited by 311
“Thanks to their capability to interact with several cellular and molecular factors as caveolae [111], viruses [125], bacteria, inflammatory molecules [126,127], and growth factors [128–130], these microdomains are involved in a plethora of biological functions, like cell polarization, membrane trafficking [111], patho…”
Background
Intracellular Lipid Flux and Membrane Microdomains as Organizing Principles in Inflammatory Cell Signaling
Fessler, M. B., & Parks, J. S. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100253 · Cited by 274
“S ince the inception of the lipid raft hypothesis in 1997 (1), a profusion of studies have reported roles for these”
Background
Structure and Mechanics of Membrane Proteins
Engel, A. H., & Gaub, H. E. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.062706.154450 · Cited by 270
The prion protein and lipid rafts (Review)
Taylor, D. R., & Hooper, N. M. (2006) · Molecular Membrane Biology · doi:10.1080/09687860500449994 · Cited by 270
Lipid rafts are involved in SARS-CoV entry into Vero E6 cells
Lu, Y., Liu, D. X., & Tam, J. P. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.02.023 · Cited by 271
“They serve as domains to concentrate membrane-associated proteins that include receptors and signaling molecules [1].”
Background
Biophysics of sphingolipids I. Membrane properties of sphingosine, ceramides and other simple sphingolipids
Goñi, F. M., & Alonso, A. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.09.011 · Cited by 269
Signalling by the RET receptor tyrosine kinase and its role in the development of the mammalian enteric nervous system
Taraviras, S. L., Marcos-Gutierrez, C. V., Durbec, P. L., Jani, H., Grigoriou, M. E., Sukumaran, M., Wang, L.-C., Hynes, M., Raisman, G., & Pachnis, V. (1999) · Development · doi:10.1242/dev.126.12.2785 · Cited by 263
GPI-microdomains: a role in signalling via immunoreceptors
Hořejšı́, V., Drbal, K., Cebecauer, M., Černý, J., Brdička, T., Angelisová, P., & Stockinger, H. S. J. (1999) · Immunology Today · doi:10.1016/s0167-5699(99)01489-9 · Cited by 269
SYMPOSIUM REVIEW: Lipid microdomains and the regulation of ion channel function
Dart, C. (2010) · The Journal of Physiology · doi:10.1113/jphysiol.2010.191585 · Cited by 273
“The lateral association of these lipids in the membrane is driven by tight hydrophilic and hydrophobic van der Waal interactions between sphingolipids and cholesterol (Simons & Ikonen, 1997).”
Hepatitis C Virus RNA Replication Occurs on a Detergent-Resistant Membrane That Cofractionates with Caveolin-2
Shi, S. T., Lee, K. J., Aizaki, H., Hwang, S. B., & Lai, M. M. C. (2003) · Journal of Virology · doi:10.1128/jvi.77.7.4160-4168.2003 · Cited by 268
Engagement of GPI-Linked CD48 Contributes to TCR Signals and Cytoskeletal Reorganization
Moran, M., & Miceli, M. C. (1998) · Immunity · doi:10.1016/s1074-7613(00)80644-5 · Cited by 267
Docosahexaenoic acid affects cell signaling by altering lipid rafts
Stillwell, W. H., Shaikh, S. R., Zerouga, M., Siddiqui, R. A., & Wassall, S. R. (2005) · annales de biologie animale biochimie biophysique · doi:10.1051/rnd:2005046 · Cited by 266
Amphitropic proteins: regulation by reversible membrane interactions (Review)
Johnson, J. E., & Cornell, R. B. (1999) · Molecular Membrane Biology · doi:10.1080/096876899294544 · Cited by 266
Characterization of the hepatitis C virus RNA replication complex associated with lipid rafts
Aizaki, H., Lee, K. J., Sung, V. M.-H., Ishiko, H., & Lai, M. M. C. (2004) · Virology · doi:10.1016/j.virol.2004.03.034 · Cited by 272
Lipid nanocarriers improve paclitaxel transport throughout human intestinal epithelial cells by using vesicle-mediated transcytosis
Roger, E., Lagarce, F., Garcion, E., & Benoît, J. (2009) · Journal of Controlled Release · doi:10.1016/j.jconrel.2009.08.010 · Cited by 265
“The caveolae-dependent or caveolae- and clathrin-independent endocytose are sphingolipid and cholesterol-rich microdomains and are referred to as ‘lipid rafts’ [57].”
Background
Invasion by Toxoplasma gondii Establishes a Moving Junction That Selectively Excludes Host Cell Plasma Membrane Proteins on the Basis of Their Membrane Anchoring
Mordue, D. G., Desai, N. N., Dustin, M. L., & Sibley, L. D. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.12.1783 · Cited by 265
Raft membrane domains: from a liquid-ordered membrane phase to a site of pathogen attack
van der Goot, F. G., & Harder, T. (2001) · Seminars in Immunology · doi:10.1006/smim.2000.0300 · Cited by 264
Ceramide function in the brain: when a slight tilt is enough
Mencarelli, C., & Martínez‐Martínez, P. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1038-x · Cited by 278
“pholipids as caveolins [138, 170] and annexins [171], respectively.”
Background
Single-particle tracking of murine polyoma virus-like particles on live cells and artificial membranes
Ewers, H., Smith, A. E., Sbalzarini, I. F., Lilie, H., Koumoutsakos, P., & Helenius, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504407102 · Cited by 264
T Cell Activation and the Cytoskeleton
Acuto, O., & Cantrell, D. A. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.165 · Cited by 264
Effect of Fengycin, a Lipopeptide Produced by Bacillus subtilis, on Model Biomembranes
Deleu, M., Paquot, M., & Nylander, T. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.114090 · Cited by 263
Ceramide-enriched membrane domains—Structure and function
Zhang, Y., Li, X., Becker, K. A., & Gulbins, E. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.07.030 · Cited by 263
Lipid rafts/caveolae as microdomains of calcium signaling
Pani, B., & Singh, B. B. (2009) · Cell Calcium · doi:10.1016/j.ceca.2009.02.009 · Cited by 263
“…activation thereby generating DAG and IP 3 . iii ) Plasma membrane lipids can also regulate trafficking of key proteins critical for Ca 2+ signaling [49,51]. iv ) In specific combinations, the lipids can assemble to form lipid rafts microdomains and thus coordinate cellular signaling [6,14,43,44].”
Background
The Continuing Mystery of Lipid Rafts
Levental, I., & Veatch, S. L. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.022 · Cited by 273
“Herein, we review recent literature on this topic with a specific focus on the major open questions in the field, including: (1) what are the best tools to assay raft behavior in living membranes; (2) what is the function of the complex lipidome of mammalian cells with respect to membrane organization; (3) what are th…”
Background
Neurons in Niemann-Pick Disease Type C Accumulate Gangliosides as Well as Unesterified Cholesterol and Undergo Dendritic and Axonal Alterations
Zervas, M., Dobrenis, K., & Walkley, S. U. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.1.49 · Cited by 262
Mechanisms of lysosomal positioning and movement
Cabukusta, B., & Neefjes, J. (2018) · Traffic · doi:10.1111/tra.12587 · Cited by 272
“It can alter membrane fluidity and form lipid microdomains in membranes.(34) While some proteins are excluded from these microdomains, others are enriched.”
Background
Specific lipid requirements of membrane proteins—a putative bottleneck in heterologous expression
Opekarová, M., & Tanner, W. (2003) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(02)00708-3 · Cited by 262
Liquid-Liquid Immiscibility in Membranes
McConnell, H. M., & Vrljic, M. (2003) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.32.110601.141704 · Cited by 262
Influenza Virus Assembly: Effect of Influenza Virus Glycoproteins on the Membrane Association of M1 Protein
Ali, A., Avalos, R. T., Ponimaskin, E. G., & Nayak, D. P. (2000) · Journal of Virology · doi:10.1128/jvi.74.18.8709-8719.2000 · Cited by 261
Characterization of Lipid Rafts from Medicago truncatula Root Plasma Membranes: A Proteomic Study Reveals the Presence of a Raft-Associated Redox System
Lefebvre, B., Furt, F., Hartmann, M.-A., Michaelson, L. V., Carde, J., Boiron, F., Rossignol, M., Napier, J. A., Cullimore, J. V., Bessoule, J., et al. (2007) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.094102 · Cited by 261
Cell wall constrains lateral diffusion of plant plasma-membrane proteins
Martinière, A., Lavagi, I., Nageswaran, G., Rolfe, D. J., Maneta-Peyret, L., Luu, D., Botchway, S. W., Webb, S. E. D., Mongrand, S., Maurel, C., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1202040109 · Cited by 260
“Numerous reports describe retarded diffusion of membrane proteins (5–8) because of structuring factors such as protein– protein interactions (9), cytoskeleton corralling (10), and lipid organization into nanodomains (11).”
Background
Beyond the lipid-bilayer: interaction of polymers and nanoparticles with membranes
Schulz, M., Olubummo, A., & Binder, W. H. (2012) · Soft Matter · doi:10.1039/c2sm06999g · Cited by 260

Authors: Simons, K., & Ikonen, E.
Affiliations: European Molecular Biology Laboratory (DE)
ORCID: Simons, Kai
Ikonen, Elina
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1997-06
Volume: 387
Issue: 6633
Pages: 569-572
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/42408
OpenAlex: W2121936687
Cited by: 9,757
References: 68
Citations by year: 2026: 168 · 2025: 188 · 2024: 208 · 2023: 223 · 2022: 240 · 2021: 263 · 2020: 293 · 2019: 274 · 2018: 278 · 2017: 289 · 2016: 312 · 2015: 344 · 2014: 343 · 2013: 347 · 2012: 388
FWCI: 18.81
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (unspecified)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
Keywords: lipid rafts, cell membrane structure, sphingolipids, cholesterol, lipid clustering, membrane fluidity, signal transduction, membrane trafficking
MeSH terms: Animals, Biological Transport, Cell Membrane, Cholesterol, Detergents, Golgi Apparatus, Humans, Membrane Lipids, Membrane Proteins, Solubility, Sphingolipids, Signal Transduction

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Functional rafts in cell membranes

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks