scholarly journals Plasma membrane rafts of rainbow trout are subject to thermal acclimation

2003 ◽  
Vol 206 (10) ◽  
pp. 1657-1667 ◽  
Author(s):  
J. K. Zehmer
2013 ◽  
Vol 368 (1611) ◽  
pp. 20120033 ◽  
Author(s):  
Enrico Klotzsch ◽  
Gerhard J. Schütz

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.


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

2003 ◽  
Vol 14 (8) ◽  
pp. 3305-3324 ◽  
Author(s):  
Sundararajan Venkatesan ◽  
Jeremy J. Rose ◽  
Robert Lodge ◽  
Philip M. Murphy ◽  
John F. Foley

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.


2009 ◽  
Vol 96 (3) ◽  
pp. 363a
Author(s):  
Mario Brameshuber ◽  
Julian Weghuber ◽  
Hannes Stockinger ◽  
Gerhard Schuetz

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

2007 ◽  
Vol 282 (48) ◽  
pp. 34994-35004 ◽  
Author(s):  
Yoshio Yamauchi ◽  
Patrick C. Reid ◽  
Jeffrey B. Sperry ◽  
Koichi Furukawa ◽  
Motohiro Takeya ◽  
...  

2004 ◽  
Vol 8 (5) ◽  
pp. 439-452 ◽  
Author(s):  
Daniel Hoessli ◽  
Isabelle Semac ◽  
Asma Iqbal ◽  
Bentham Science Publisher Nasir-ud-Din ◽  
Bettina Borisch

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