scholarly journals Controlling transmembrane protein concentration and orientation in supported lipid bilayers

2017 ◽  
Vol 53 (30) ◽  
pp. 4250-4253 ◽  
Author(s):  
P. Bao ◽  
M. L. Cartron ◽  
K. H. Sheikh ◽  
B. R. G. Johnson ◽  
C. N. Hunter ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Lipid Bilayers ◽  
Electric Fields ◽  
Protein Concentration ◽  
Transmembrane Protein ◽  
Fold Increase ◽  
Supported Lipid Bilayers

The trans-membrane protein–proteorhodopsin (pR) has been incorporated into supported lipid bilayers (SLB). In-plane electric fields have been used to manipulate the orientation and concentration of these proteins, within the SLB, through electrophoresis leading to a 25-fold increase concentration of pR.

Peptide Disc Mediated Control of Membrane Protein Orientation in Supported Lipid Bilayers for Surface-Sensitive Investigations

2019 ◽  
Vol 92 (1) ◽  
pp. 1081-1088 ◽  
Author(s):  
Alessandra Luchini ◽  
Frederik Grønbæk Tidemand ◽  
Nicolai Tidemand Johansen ◽  
Mario Campana ◽  
Javier Sotres ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Lipid Bilayers ◽  
Supported Lipid Bilayers ◽  
Protein Orientation

Single-Molecule Detection with Lightguiding Nanowires: Determination of Protein Concentration and Diffusivity in Supported Lipid Bilayers

Nano Letters ◽  
2019 ◽  
Vol 19 (9) ◽  
pp. 6182-6191 ◽  
Author(s):  
Damiano Verardo ◽  
Björn Agnarsson ◽  
Vladimir P. Zhdanov ◽  
Fredrik Höök ◽  
Heiner Linke
Keyword(s):  
Lipid Bilayers ◽  
Single Molecule ◽  
Protein Concentration ◽  
Single Molecule Detection ◽  
Supported Lipid Bilayers

Preserved Transmembrane Protein Mobility in Polymer-Supported Lipid Bilayers Derived from Cell Membranes

2015 ◽  
Vol 87 (18) ◽  
pp. 9194-9203 ◽  
Author(s):  
Hudson Pace ◽  
Lisa Simonsson Nyström ◽  
Anders Gunnarsson ◽  
Elizabeth Eck ◽  
Christopher Monson ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Cell Membranes ◽  
Transmembrane Protein ◽  
Supported Lipid Bilayers ◽  
Protein Mobility ◽  
Polymer Supported

Electrophoretic mobility of a monotopic membrane protein inserted into the top of supported lipid bilayers

2016 ◽  
Vol 39 (12) ◽  
Author(s):  
Frédéric Harb ◽  
Marie-Thérèse Giudici-Orticoni ◽  
Marianne Guiral ◽  
Bernard Tinland
Keyword(s):  
Membrane Protein ◽  
Electrophoretic Mobility ◽  
Lipid Bilayers ◽  
Supported Lipid Bilayers

Exploration of interactions between membrane proteins embedded in supported lipid bilayers and their antibodies by reflectometric interference spectroscopy-based sensing

The Analyst ◽  
2014 ◽  
Vol 139 (22) ◽  
pp. 6016-6021 ◽  
Author(s):  
Yoshikazu Kurihara ◽  
Tsuneo Sawazumi ◽  
Toshifumi Takeuchi
Keyword(s):  
Multidrug Resistance ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Lipid Bilayers ◽  
Model Membrane ◽  
Supported Lipid Bilayers ◽  
Reflectometric Interference Spectroscopy

A microfluidic reflectometric interference spectroscopy (RIfS)-based sensor was fabricated to investigate the activity of multidrug resistance-associated protein 1 (MRP1), applied as a model membrane protein.

scholarly journals IgG surface mobility promotes antibody-dependent cellular phagocytosis by Syk and Arp2/3 mediated reorganization of Fcγ receptors in macrophages.

2021 ◽  
Author(s):  
Seongwan Jo ◽  
Nicholas M. Cronin ◽  
Ni Putu Dewi Nurmalasari ◽  
Jason G. Kerkvleit ◽  
Elizabeth M. Bailey ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Target Cell ◽  
Transmembrane Protein ◽  
Supported Lipid Bilayers ◽  
Fcγ Receptors ◽  
Lymphoma Cells ◽  
Antigenic Modulation ◽  
B Lymphoma ◽  
Surface Mobility ◽  
B Lymphoma Cells

By visualizing the movements of Rituximab during Antibody dependent cellular phagocytosis (ADCP) of B lymphoma cells by macrophages, we found that Fcγ receptors (FcγR) on the macrophage surface microcluster, recruit Syk and undergro large-scale reorganization at the phagocytic synapse prior to and during engulfment of the target cell. Given these dramatic rearrangements, we analyzed how the surface mobility of Rituximab contributes to FcγR signal amplification and ADCP efficiency. Depolymerization of the target cell actin cytoskeleton resulted in free diffusion of Rituximab docked to CD20, enhanced microcluster reorganization, Syk recruitment and ADCP. Conversely, immobilization of Rituximab by chemical fixation impaired microcluster formation and diminished Syk recruitment and ADCP. In macrophages lacking Syk, Rituximab accumulated at the base of the phagosome and were trogocytosed, consistent with Syk kinase activity being necessary to trigger the redistribution of Rituximab-FcγR during engulfment and to prevent antigenic modulation of the target. Total internal reflection fluorescence analysis of FcγR-IgG on fluid supported lipid bilayers revealed a membrane topography displaying inward reaching leading edges and protruding contact sites reminiscent of podosomes. This topography was distinct from the closely apposed macrophage/target membranes observed during engagement of IgG displayed on immobile supported lipid bilayers. The organization of this contact, pseudopod extension and the rearrangement of microclusters depended critically on Arp 2/3. Thus, Syk and Arp2/3 coordinate actin rearrangements and FcγR-IgG complexes that were of previously unrecognized complexity for the clearance of cells displaying surface-mobile antigens. ADCP is an important effector mechanism for the removal of malignant, immunologically aberrant, and infected cells during treatment with therapeutic antibodies or adaptive immune responses. Most transmembrane protein antigens are mobile with transient confinement from the actin of the target cell. This work demonstrates that macrophage forces overcome these confinements to rearrange FcγR-IgG-antigen complexes before and during ADCP. Thus, new paradigms are needed as ADCP has largely been studied using model target particles that display immobile antigens. Moreover, we found that the mobility of the therapeutic antibody, Rituximab, on the surface of B lymphoma cells foretells ADCP efficacy, with lower densities of IgG mediating ADCP on increasingly mobile antigens.

Charge-selective membrane protein patterning with proteoliposomes

RSC Advances ◽  
2015 ◽  
Vol 5 (7) ◽  
pp. 5183-5191
Author(s):  
Heesuk Kim ◽  
Keel Yong Lee ◽  
Soo Ryeon Ryu ◽  
Kwang-Hwan Jung ◽  
Tae Kyu Ahn ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Lipid Bilayers ◽  
Transmembrane Protein ◽  
Protein Patterning ◽  
Lipid Layer ◽  
Selective Membrane ◽  
Novel Method

A novel method to fabricate transmembrane protein (TP) embedded lipid bilayers has been developed, resulting in an immobilized, but biologically functioning TP embedded lipid layer precisely in the targeted patterns.

scholarly journals Unraveling membrane properties at the organelle-level with LipidDyn

2022 ◽  
Author(s):  
Simone Scrima ◽  
Matteo Tiberti ◽  
Alessia Campo ◽  
Elisabeth Corcelle-Termeau ◽  
Delphine Judith ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Lipid Bilayers ◽  
Protein Interactions ◽  
Transmembrane Protein ◽  
Md Simulations ◽  
Membrane Properties ◽  
Cellular Membranes ◽  
Simulation Data ◽  
Membrane Function ◽  
Cellular Environment

Cellular membranes are formed from many different lipids in various amounts and proportions depending on the subcellular localization. The lipid composition of membranes is sensitive to changes in the cellular environment, and their alterations are linked to several diseases, including cancer. Lipids not only form lipid-lipid interactions but also interact with other biomolecules, including proteins, profoundly impacting each other. Molecular dynamics (MD) simulations are a powerful tool to study the properties of cellular membranes and membrane-protein interactions on different timescales and at varying levels of resolution. Over the last few years, software and hardware for biomolecular simulations have been optimized to routinely run long simulations of large and complex biological systems. On the other hand, high-throughput techniques based on lipidomics provide accurate estimates of the composition of cellular membranes at the level of subcellular compartments. The community needs computational tools for lipidomics and simulation data effectively interacting to better understand how changes in lipid compositions impact membrane function and structure. Lipidomic data can be analyzed to design biologically relevant models of membranes for MD simulations. Similar applications easily result in a massive amount of simulation data where the bottleneck becomes the analysis of the data to understand how membrane properties and membrane-protein interactions are changing in the different conditions. In this context, we developed LipidDyn, an in silico pipeline to streamline the analyses of MD simulations of membranes of different compositions. Once the simulations are collected, LipidDyn provides average properties and time series for several membrane properties such as area per lipid, thickness, diffusion motions, the density of lipid bilayers, and lipid enrichment/depletion. The calculations exploit parallelization and the pipelines include graphical outputs in a publication-ready form. We applied LipidDyn to different case studies to illustrate its potential, including membranes from cellular compartments and transmembrane protein domains. LipidDyn is implemented in Python and relies on open-source libraries. LipidDyn is available free of charge under the GNU General Public License from https://github.com/ELELAB/LipidDyn.

scholarly journals Membrane surfaces regulate assembly of a ribonucleoprotein condensate

2021 ◽  
Author(s):  
Wilton T. Snead ◽  
Therese M. Gerbich ◽  
Ian Seim ◽  
Zhongxiu Hu ◽  
Amy S. Gladfelter
Keyword(s):  
Lipid Bilayers ◽  
Protein Concentration ◽  
Membrane Surface ◽  
Supported Lipid Bilayers ◽  
Size Distributions ◽  
Membrane Surfaces ◽  
Diffusion Rates ◽  
Lipid Surface ◽  
Rna Complexes ◽  
In Cells

AbstractBiomolecular condensates organize biochemistry in time and space, yet little is known about how cells control either the position or scale of these assemblies. In cells, condensates often appear as dispersed, relatively small assemblies that do not grow (coarsen) into a single droplet despite their propensity to coalesce. Here we report that ribonucleoprotein condensates of the Q-rich protein Whi3 interact with the endoplasmic reticulum, prompting us to hypothesize that membrane association controls the position and size of condensates. Reconstitution of Whi3 condensates on supported lipid bilayers reveals that association with a diffusive lipid surface promotes condensation at both physiological ionic strength and protein concentration. Notably, these assemblies rapidly arrest, matching size distributions seen in cells. The timing of the arrest is influenced by the ordering of protein-protein and protein-RNA interactions and controlled by the slow diffusion of complexes induced by the membrane. This slowed diffusion limits both transfer of small protein-RNA complexes between condensates and their coalescence, thus driving coarsening to arrest. Our experiments reveal a tradeoff between locally-enhanced protein concentration at membranes, which favors condensation, and an accompanying reduction in diffusion, which restricts coarsening. Thus, membranes can maintain a population of small condensates in the absence of active mechanisms. Given that many condensates are bound to endomembranes, we predict that the biophysical properties of lipid bilayers are key for controlling condensate sizes throughout the cell.One sentence summaryAssembly on a membrane surface positions and scales biomolecular condensates by controlling relative diffusion rates of proteins and nucleic acids.

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