scholarly journals A critical survey of methods to detect plasma membrane rafts

2013 ◽  
Vol 368 (1611) ◽  
pp. 20120033 ◽  
Author(s):  
Enrico Klotzsch ◽  
Gerhard J. Schütz
Keyword(s):  
Plasma Membrane ◽  
Single Molecule ◽  
Cellular Structures ◽  
Good Time ◽  
Membrane Rafts ◽  
Critical Survey ◽  
Membrane Models ◽  
Plasma Membrane Rafts ◽  
Resolution Single ◽  
Experimental Strategies

The plasma membrane is still one of the enigmatic cellular structures. Although the microscopic structure is getting clearer, not much is known about the organization at the nanometre level. Experimental difficulties have precluded unambiguous approaches, making the current picture rather fuzzy. In consequence, a variety of different membrane models has been proposed over the years, on the basis of different experimental strategies. Recent data obtained via high-resolution single-molecule microscopy shed new light on the existing hypotheses. We thus think it is a good time for reviewing the consistency of the existing models with the new data. In this paper, we summarize the available models in ten propositions, each of which is discussed critically with respect to the applied technologies and the strengths and weaknesses of the approaches. Our aim is to provide the reader with a sound basis for his own assessment. We close this chapter by exposing our picture of the membrane organization at the nanoscale.

scholarly journals Direct Observation Of Plasma Membrane Rafts Via Live Cell Single Molecule Microscopy

2009 ◽  
Vol 96 (3) ◽  
pp. 363a
Author(s):  
Mario Brameshuber ◽  
Julian Weghuber ◽  
Hannes Stockinger ◽  
Gerhard Schuetz
Keyword(s):  
Plasma Membrane ◽  
Direct Observation ◽  
Single Molecule ◽  
Live Cell ◽  
Membrane Rafts ◽  
Single Molecule Microscopy ◽  
Plasma Membrane Rafts

scholarly journals Single-molecule imaging of HIV-1 envelope glycoprotein dynamics and Gag lattice association exposes determinants responsible for virus incorporation

2019 ◽  
Vol 116 (50) ◽  
pp. 25269-25277 ◽  
Author(s):  
Nairi Pezeshkian ◽  
Nicholas S. Groves ◽  
Schuyler B. van Engelenburg
Keyword(s):  
Plasma Membrane ◽  
Single Molecule ◽  
Envelope Glycoprotein ◽  
Virus Assembly ◽  
Single Molecule Tracking ◽  
Virus Particles ◽  
Cell Plasma ◽  
The Matrix ◽  
Resolution Single ◽  
Hiv 1

The HIV-1 envelope glycoprotein (Env) is sparsely incorporated onto assembling virus particles on the host cell plasma membrane in order for the virus to balance infectivity and evade the immune response. Env becomes trapped in a nascent particle on encounter with the polymeric viral protein Gag, which forms a dense protein lattice on the inner leaflet of the plasma membrane. While Env incorporation efficiency is readily measured biochemically from released particles, very little is known about the spatiotemporal dynamics of Env trapping events. Herein, we demonstrate, via high-resolution single-molecule tracking, that retention of Env trimers within single virus assembly sites requires the Env cytoplasmic tail (CT) and the L12 residue in the matrix (MA) domain of Gag but does not require curvature of the viral lattice. We further demonstrate that Env trimers are confined to subviral regions of a budding Gag lattice, supporting a model where direct interactions and/or steric corralling between the Env-CT and a lattice of MA trimers promote Env trapping and infectious HIV-1 assembly.

scholarly journals (Un)Confined Diffusion of CD59 in the Plasma Membrane Determined by High-Resolution Single Molecule Microscopy

2007 ◽  
Vol 92 (10) ◽  
pp. 3719-3728 ◽  
Author(s):  
Stefan Wieser ◽  
Manuel Moertelmaier ◽  
Elke Fuertbauer ◽  
Hannes Stockinger ◽  
Gerhard J. Schütz
Keyword(s):  
Plasma Membrane ◽  
High Resolution ◽  
Single Molecule ◽  
Single Molecule Microscopy ◽  
Resolution Single

Oxysterols: Influence on plasma membrane rafts microdomains and development of ocular diseases

Steroids ◽  
2015 ◽  
Vol 99 ◽  
pp. 259-265 ◽  
Author(s):  
Rodolphe Filomenko ◽  
Cynthia Fourgeux ◽  
Lionel Bretillon ◽  
Ségolène Gambert-Nicot
Keyword(s):  
Plasma Membrane ◽  
Membrane Rafts ◽  
Ocular Diseases ◽  
Plasma Membrane Rafts

scholarly journals Distinct Mechanisms of Agonist-induced Endocytosis for Human Chemokine Receptors CCR5 and CXCR4

2003 ◽  
Vol 14 (8) ◽  
pp. 3305-3324 ◽  
Author(s):  
Sundararajan Venkatesan ◽  
Jeremy J. Rose ◽  
Robert Lodge ◽  
Philip M. Murphy ◽  
John F. Foley
Keyword(s):  
Plasma Membrane ◽  
Chemokine Receptors ◽  
G Protein Coupled Receptors ◽  
Membrane Rafts ◽  
Expression Systems ◽  
Receptor Endocytosis ◽  
Plasma Membrane Rafts ◽  
G Protein Coupled ◽  
Transmission Of Disease ◽  
Dependent Pathway

Desensitization of the chemokine receptors, a large class of G protein–coupled receptors, is mediated in part by agonist-driven receptor endocytosis. However, the exact pathways have not been fully defined. Here we demonstrate that the rate of ligand-induced endocytosis of CCR5 in leukocytes and expression systems is significantly slower than that of CXCR4 and requires prolonged agonist treatment, suggesting that these two receptors use distinct mechanisms. We show that the C-terminal domain of CCR5 is the determinant of its slow endocytosis phenotype. When the C-tail of CXCR4 was exchanged for that of CCR5, the resulting CXCR4-CCR5 (X4-R5) chimera displayed a CCR5-like trafficking phenotype. We found that the palmitoylated cysteine residues in this domain anchor CCR5 to plasma membrane rafts. CXCR4 and a C-terminally truncated CCR5 mutant (CCR5-KRFX) lacking these cysteines are not raft associated and are endocytosed by a clathrin-dependent pathway. Genetic inhibition of clathrin-mediated endocytosis demonstrated that a significant fraction of ligand-occupied CCR5 trafficked by clathrin-independent routes into caveolin-containing vesicular structures. Thus, the palmitoylated C-tail of CCR5 is the major determinant of its raft association and endocytic itineraries, differentiating it from CXCR4 and other chemokine receptors. This novel feature of CCR5 may modulate its signaling potential and could explain its preferential use by HIV for person-to-person transmission of disease.

Chimeric GnRH–LH receptors and LH receptors lacking C-terminus palmitoylation sites do not localize to plasma membrane rafts

2005 ◽  
Vol 337 (2) ◽  
pp. 430-434 ◽  
Author(s):  
Ying Lei ◽  
Guy M. Hagen ◽  
Steven M.L. Smith ◽  
B. George Barisas ◽  
Deborah A. Roess
Keyword(s):  
Plasma Membrane ◽  
Membrane Rafts ◽  
C Terminus ◽  
Plasma Membrane Rafts
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