scholarly journals Detergent-resistant membrane domains but not the proteasome are involved in the misfolding of a PrP mutant retained in the endoplasmic reticulum

2006 ◽  
Vol 119 (3) ◽  
pp. 433-442 ◽  
Author(s):  
V. Campana
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Domains ◽  
Detergent Resistant Membrane

scholarly journals Proteomic Analysis of Detergent Resistant Membrane Domains during Early Interaction of Macrophages with Rough and Smooth Brucella melitensis

PLoS ONE ◽  
2014 ◽  
Vol 9 (3) ◽  
pp. e91706 ◽  
Author(s):  
Sabine A. Lauer ◽  
Srinivas Iyer ◽  
Timothy Sanchez ◽  
Christian V. Forst ◽  
Brent Bowden ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Brucella Melitensis ◽  
Membrane Domains ◽  
Early Interaction ◽  
Detergent Resistant Membrane

scholarly journals Cdc42 regulates neutrophil migration via crosstalk between WASp, CD11b, and microtubules

Blood ◽  
2012 ◽  
Vol 120 (17) ◽  
pp. 3563-3574 ◽  
Author(s):  
Sachin Kumar ◽  
Juying Xu ◽  
Charles Perkins ◽  
Fukun Guo ◽  
Scott Snapper ◽  
...  
Keyword(s):  
Rho Gtpase ◽  
Neutrophil Migration ◽  
Cell Polarization ◽  
Membrane Domains ◽  
Long Distance ◽  
Cellular Defense ◽  
Persistent Cell ◽  
Proper Balance ◽  
Detergent Resistant Membrane ◽  
Standing Question

Abstract Chemotaxis promotes neutrophil participation in cellular defense by enabling neutrophil migration to infected tissue and is controlled by persistent cell polarization. One long-standing question of neutrophil polarity has been how the pseudopod and the uropod are coordinated. In our previous report, we suggested that Rho GTPase Cdc42 controls neutrophil polarity through CD11b signaling at the uropod, albeit through an unknown mechanism. Here, we show that Cdc42 controls polarity, unexpectedly, via its effector WASp. Cdc42 controls WASp activation and its distant localization to the uropod. At the uropod, WASp regulates the reorganization of CD11b integrin into detergent resistant membrane domains; in turn, CD11b recruits the microtubule end binding protein EB1 to capture and stabilize microtubules at the uropod. This organization is necessary to maintain neutrophil polarity during migration and is critical for neutrophil emigration into inflamed lungs. These results suggest unrecognized mechanism of neutrophil polarity in which WASp mediates long-distance control of the uropod by Cdc42 to maintain a proper balance between the pseudopod and the uropod. Our study reveals a new function for WASp in the control of neutrophil polarity via crosstalk between CD11b and microtubules.

Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains

PROTEOMICS ◽  
2001 ◽  
Vol 1 (8) ◽  
pp. 1010-1021 ◽  
Author(s):  
Priska D. von Haller ◽  
Sam Donohoe ◽  
David R. Goodlett ◽  
Ruedi Aebersold ◽  
Julian D. Watts
Keyword(s):  
T Cell ◽  
Mass Spectrometric ◽  
Membrane Domains ◽  
Jurkat T Cell ◽  
Detergent Resistant Membrane

The presence of an ER exit signal determines the protein sorting upon ER exit in yeast

2008 ◽  
Vol 414 (2) ◽  
pp. 237-245 ◽  
Author(s):  
Reika Watanabe ◽  
Guillaume A. Castillon ◽  
Anja Meury ◽  
Howard Riezman
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Sorting ◽  
Surface Protein ◽  
The Other ◽  
Gpi Anchor ◽  
Rich Region ◽  
Characteristic Features ◽  
Detergent Resistant Membrane

In yeast, there are at least two vesicle populations upon ER (endoplasmic reticulum) exit, one containing Gap1p (general aminoacid permease) and a glycosylated α-factor, gpαF (glycosylated proα-factor), and the other containing GPI (glycosylphosphatidylinositol)-anchored proteins, Gas1p (glycophospholipid-anchored surface protein) and Yps1p. We attempted to identify sorting determinants for this protein sorting event in the ER. We found that mutant Gas1 proteins that lack a GPI anchor and/or S/T region (serine- and threonine-rich region), two common characteristic features conserved among yeast GPI-anchored proteins, were still sorted away from Gap1p-containing vesicles. Furthermore, a mutant glycosylated α-factor, gpαGPI, which contains both the GPI anchor and S/T region from Gas1p, still entered Gap1p-containing vesicles, demonstrating that these conserved characteristics do not prevent proteins from entering Gap1p-containing vesicles. gpαF showed severely reduced budding efficiency in the absence of its ER exit receptor Erv29p, and this residual budding product no longer entered Gap1p-containing vesicles. These results suggest that the interaction of gpαF with Erv29p is essential for sorting into Gap1p-containing vesicles. We compared the detergent solubility of Gas1p and the gpαGPI in the ER with that in ER-derived vesicles. Both GPI-anchored proteins similarly partitioned into the DRM (detergent-resistant membrane) in the ER. Based on the fact that they entered different ER-derived vesicles, we conclude that DRM partitioning of GPI-anchored proteins is not the dominant determinant of protein sorting upon ER exit. Interestingly, upon incorporation into the ER-derived vesicles, gpαGPI was no longer detergent-insoluble, in contrast with the persistent detergent insolubility of Gas1p in the ER-derived vesicles. We present different explanations for the different behaviours of GPI-anchored proteins in distinct ER-derived vesicle populations.

scholarly journals Cytoskeleton-dependent Membrane Domain Segregation during Neutrophil Polarization

2001 ◽  
Vol 12 (11) ◽  
pp. 3550-3562 ◽  
Author(s):  
Stéphanie Seveau ◽  
Robert J. Eddy ◽  
Frederick R. Maxfield ◽  
Lynda M. Pierini
Keyword(s):  
Plasma Membrane ◽  
Myosin Light Chain ◽  
Transmembrane Proteins ◽  
Cell Polarization ◽  
Membrane Domains ◽  
Membrane Domain ◽  
Actin Remodeling ◽  
Cytoskeletal Rearrangements ◽  
Triton X ◽  
Detergent Resistant Membrane

On treatment with chemoattractant, the neutrophil plasma membrane becomes organized into detergent-resistant membrane domains (DRMs), the distribution of which is intimately correlated with cell polarization. Plasma membrane at the front of polarized cells is susceptible to extraction by cold Triton X-100, whereas membrane at the rear is resistant to extraction. After cold Triton X-100 extraction, DRM components, including the transmembrane proteins CD44 and CD43, the GPI-linked CD16, and the lipid analog, DiIC16, are retained within uropods and cell bodies. Furthermore, CD44 and CD43 interact concomitantly with DRMs and with the F-actin cytoskeleton, suggesting a mechanism for the formation and stabilization of DRMs. By tracking the distribution of DRMs during polarization, we demonstrate that DRMs progress from a uniform distribution in unstimulated cells to small, discrete patches immediately after activation. Within 1 min, DRMs form a large cap comprising the cell body and uropod. This process is dependent on myosin in that an inhibitor of myosin light chain kinase can arrest DRM reorganization and cell polarization. Colabeling DRMs and F-actin revealed a correlation between DRM distribution and F-actin remodeling, suggesting that plasma membrane organization may orient signaling events that control cytoskeletal rearrangements and, consequently, cell polarity.

The effect of simvastatin on the proteome of detergent-resistant membrane domains: Decreases of specific proteins previously related to cytoskeleton regulation, calcium homeostasis and cell fate

PROTEOMICS ◽  
2010 ◽  
Vol 10 (10) ◽  
pp. 1954-1965 ◽  
Author(s):  
Jovita Ponce ◽  
David Brea ◽  
Montserrat Carrascal ◽  
Verónica Guirao ◽  
Nuria DeGregorio-Rocasolano ◽  
...  
Keyword(s):  
Cell Fate ◽  
Calcium Homeostasis ◽  
Membrane Domains ◽  
Specific Proteins ◽  
Detergent Resistant Membrane

scholarly journals Detergent Resistant Membrane Domains in Broccoli Plasma Membrane Associated to the Response to Salinity Stress

2020 ◽  
Vol 21 (20) ◽  
pp. 7694
Author(s):  
Lucía Yepes-Molina ◽  
Micaela Carvajal ◽  
Maria Carmen Martínez-Ballesta
Keyword(s):  
Plasma Membrane ◽  
Membrane Trafficking ◽  
Lower Amount ◽  
Membrane Domains ◽  
Cellular Functions ◽  
Osmotic Water ◽  
Fatty Acid Saturation ◽  
Protein Partitioning ◽  
Detergent Resistant Membranes ◽  
Detergent Resistant Membrane

Detergent-resistant membranes (DRMs) microdomains, or “raft lipids”, are key components of the plasma membrane (PM), being involved in membrane trafficking, signal transduction, cell wall metabolism or endocytosis. Proteins imbibed in these domains play important roles in these cellular functions, but there are few studies concerning DRMs under abiotic stress. In this work, we determine DRMs from the PM of broccoli roots, the lipid and protein content, the vesicles structure, their water osmotic permeability and a proteomic characterization focused mainly in aquaporin isoforms under salinity (80 mM NaCl). Based on biochemical lipid composition, higher fatty acid saturation and enriched sterol content under stress resulted in membranes, which decreased osmotic water permeability with regard to other PM vesicles, but this permeability was maintained under control and saline conditions; this maintenance may be related to a lower amount of total PIP1 and PIP2. Selective aquaporin isoforms related to the stress response such as PIP1;2 and PIP2;7 were found in DRMs and this protein partitioning may act as a mechanism to regulate aquaporins involved in the response to salt stress. Other proteins related to protein synthesis, metabolism and energy were identified in DRMs independently of the treatment, indicating their preference to organize in DMRs.

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