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 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.

scholarly journals Reticulon Protein-1C: A New Hope in the Treatment of Different Neuronal Diseases

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Federica Di Sano ◽  
Mauro Piacentini
Keyword(s):  
Cell Death ◽  
Membrane Proteins ◽  
Neurodegenerative Diseases ◽  
Er Stress ◽  
Calcium Homeostasis ◽  
Neurodegenerative Disorders ◽  
Cellular Functions ◽  
Promising Target ◽  
Specific Proteins ◽  
Structure And Functions

Reticulons (RTNs) are a group of membrane proteins localized on the ER and known to regulate ER structure and functions. Several studies have suggested that RTNs are involved in different important cellular functions such as changes in calcium homeostasis, ER-stress-mediated cell death, and autophagy. RTNs have been demonstrated to exert a cancer specific proapoptotic function via the interaction or the modulation of specific proteins. Reticulons have also been implicated in different signaling pathways which are at the basis of the pathogenesis of several neurodegenerative diseases. In this paper we discuss the accumulating evidence identifying RTN-1C protein as a promising target in the treatment of different pathologies such as cancer or neurodegenerative disorders.

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

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.

Postsynaptic nanodomains generated by local palmitoylation cycles

2015 ◽  
Vol 43 (2) ◽  
pp. 199-204 ◽  
Author(s):  
Masaki Fukata ◽  
Atsushi Sekiya ◽  
Tatsuro Murakami ◽  
Norihiko Yokoi ◽  
Yuko Fukata
Keyword(s):  
Plasma Membrane ◽  
Protein Targeting ◽  
Scaffolding Protein ◽  
Dependent Manner ◽  
Membrane Domains ◽  
Post Translational Modification ◽  
Cellular Functions ◽  
Protein Palmitoylation ◽  
Specific Proteins

Precise regulation of protein assembly at specialized membrane domains is essential for diverse cellular functions including synaptic transmission. However, it is incompletely understood how protein clustering at the plasma membrane is initiated, maintained and controlled. Protein palmitoylation, a common post-translational modification, regulates protein targeting to the plasma membrane. Such modified proteins are enriched in these specialized membrane domains. In this review, we focus on palmitoylation of PSD-95, which is a major postsynaptic scaffolding protein and makes discrete postsynaptic nanodomains in a palmitoylation-dependent manner and discuss a determinant role of local palmitoylation cycles in creating highly localized hotspots at the membrane where specific proteins concentrate to organize functional domains.

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