
@article {3560,
	title = {GPI-anchored protein organization and dynamics at the cell surface.},
	journal = {J Lipid Res},
	volume = {57},
	year = {2016},
	month = {2016 Feb},
	pages = {159-75},
	abstract = {<p>The surface of eukaryotic cells is a multi-component fluid bilayer in which glycosylphosphatidylinositol (GPI)-anchored proteins are an abundant constituent. In this review, we discuss the complex nature of the organization and dynamics of GPI-anchored proteins at multiple spatial and temporal scales. Different biophysical techniques have been utilized for understanding this organization, including fluorescence correlation spectroscopy, fluorescence recovery after photobleaching, single particle tracking, and a number of super resolution methods. Major insights into the organization and dynamics have also come from exploring the short-range interactions of GPI-anchored proteins by fluorescence (or F{\"o}rster) resonance energy transfer microscopy. Based on the nanometer to micron scale organization, at the microsecond to the second time scale dynamics, a picture of the membrane bilayer emerges where the lipid bilayer appears inextricably intertwined with the underlying dynamic cytoskeleton. These observations have prompted a revision of the current models of plasma membrane organization, and suggest an active actin-membrane composite.</p>
},
	issn = {1539-7262},
	doi = {10.1194/jlr.R062885},
	author = {Saha, Suvrajit and Anilkumar, Anupama Ambika and Mayor, Satyajit}
}
