Journal
JOURNAL OF LIPID RESEARCH
Volume 57, Issue 2, Pages 159-175Publisher
ELSEVIER
DOI: 10.1194/jlr.R062885
Keywords
lipid rafts; glycosylphosphatidylinositolanchored protein; nanoscale; diffusion; homo-fluorescence resonance energy transfer; super-resolution; signal transduction; microdomains; actomyosin; activity
Categories
Funding
- Human Frontier Science Program Grant [RGP0027/2012]
- NCBS-TIFR graduate program
- Council of Scientific and Industrial Research, Government of India
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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 Forster) 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.
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