GPI-anchored protein organization and dynamics at the cell surface.
|Title||GPI-anchored protein organization and dynamics at the cell surface.|
|Publication Type||Journal Article|
|Year of Publication||2016|
|Authors||Saha S, Anilkumar AAmbika, Mayor S|
|Journal||J Lipid Res|
|Date Published||2016 Feb|
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 Förster) 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.
|Alternate Journal||J. Lipid Res.|
|PubMed Central ID||PMC4727430|