
@article {863,
	title = {Homo-FRET imaging highlights the nanoscale organization of cell surface molecules.},
	journal = {Methods Mol Biol},
	volume = {1251},
	year = {2015},
	month = {2015},
	pages = {151-73},
	abstract = {<p>Several models have been proposed to understand the structure and organization of the plasma membrane in living cells. Predicated on equilibrium thermodynamic principles, the fluid-mosaic model of Singer and Nicholson and the model of lipid domains (or membrane rafts) are dominant models, which account for a fluid bilayer and functional lateral heterogeneity of membrane components, respectively. However, the constituents of the membrane and its composition are not maintained by equilibrium mechanisms. Indeed, the living cell membrane is a steady state of a number of active processes, namely, exocytosis, lipid synthesis and transbilayer flip-flop, and endocytosis. In this active milieu, many lipid constituents of the cell membrane exhibit a nanoscale organization that is also at odds with passive models based on chemical equilibrium. Here we provide a detailed description of microscopy and cell biological methods that have served to provide valuable information regarding the nature of nanoscale organization of lipid components in a living cell.</p>
},
	keywords = {Animals, Cell Membrane, CHO Cells, Cricetinae, Cricetulus, Fluorescence Polarization, Fluorescence Resonance Energy Transfer, Lipid Bilayers, Microscopy, Fluorescence, Models, Biological, Nanotechnology},
	issn = {1940-6029},
	doi = {10.1007/978-1-4939-2080-8_9},
	author = {Saha, Suvrajit and Raghupathy, Riya and Mayor, Satyajit}
}
@article {881,
	title = {Transbilayer lipid interactions mediate nanoclustering of lipid-anchored proteins.},
	journal = {Cell},
	volume = {161},
	year = {2015},
	month = {2015 Apr 23},
	pages = {581-94},
	abstract = {<p>Understanding how functional lipid domains in live cell membranes are generated has posed a challenge. Here, we show that transbilayer interactions are necessary for the generation of cholesterol-dependent nanoclusters of GPI-anchored proteins mediated by membrane-adjacent dynamic actin filaments. We find that long saturated acyl-chains are required for forming GPI-anchor nanoclusters. Simultaneously, at the inner leaflet, long acyl-chain-containing phosphatidylserine (PS) is necessary for transbilayer coupling. All-atom molecular dynamics simulations of asymmetric multicomponent-membrane bilayers in a mixed phase provide evidence that immobilization of long saturated acyl-chain lipids at either leaflet stabilizes cholesterol-dependent transbilayer interactions forming local domains with characteristics similar to a liquid-ordered (lo) phase. This is verified by experiments wherein immobilization of long acyl-chain lipids at one leaflet effects transbilayer interactions of corresponding lipids at the opposite leaflet. This suggests a general mechanism for the generation and stabilization of nanoscale cholesterol-dependent and actin-mediated lipid clusters in live cell membranes.</p>
},
	keywords = {Actins, Animals, Cell Membrane, CHO Cells, Cricetulus, Glycosylphosphatidylinositols, Lipid-Linked Proteins, Molecular Dynamics Simulation, Phosphatidylserines},
	issn = {1097-4172},
	doi = {10.1016/j.cell.2015.03.048},
	author = {Raghupathy, Riya and Anilkumar, Anupama Ambika and Polley, Anirban and Singh, Parvinder Pal and Yadav, Mahipal and Johnson, Charles and Suryawanshi, Sharad and Saikam, Varma and Sawant, Sanghapal D and Panda, Aniruddha and Guo, Zhongwu and Vishwakarma, Ram A and Rao, Madan and Mayor, Satyajit}
}
