Image Correlation Spectroscopy
- 18 December 2007
- journal article
- protocols
- Published by American Association for the Advancement of Science (AAAS) in Science's STKE
- Vol. 2007 (417), pl7
- https://doi.org/10.1126/stke.4172007pl7
Abstract
Membrane domains, such as caveolae and clathrin-coated pits, regulate cell signaling and protein internalization in the plasma membrane. Fluorescence imaging and microscopy provide an opportunity to determine the receptor protein dynamics of membrane microdomains. The family of image correlation spectroscopy (ICS) techniques provides powerful tools with which to measure the aggregation, clustering, and dynamics of proteins in the plasma membrane. ICS is used to calculate the cluster density and the degree of aggregation of plasma membrane proteins, whereas image cross-correlation spectroscopy (ICCS) measures the fraction of colocalization of two proteins. Dynamic image correlation spectroscopy (DICS) can be used to analyze protein dynamics on the cell surface during live-cell imaging.Keywords
This publication has 38 references indexed in Scilit:
- Caveolae, Lipid Rafts, and Vascular DiseaseTrends in Cardiovascular Medicine, 2005
- Caveolins, caveolae, and lipid rafts in cellular transport, signaling, and diseaseBiochemistry and Cell Biology, 2004
- Fluorescence correlation spectroscopy and quantitative cell biologyDifferentiation, 2004
- Quick tour of fluorescence correlation spectroscopy from its inceptionJournal of Biomedical Optics, 2004
- Caveosomes and endocytosis of lipid raftsJournal of Cell Science, 2003
- Clathrin-mediated endocytosis in AP-2–depleted cellsThe Journal of cell biology, 2003
- Fluorescence correlation spectroscopy for the detection and study of single molecules in biologyBioEssays, 2002
- Fluorescence correlation spectroscopy: molecular recognition at the single molecule levelJournal of Molecular Recognition, 2000
- Caveolae, DIGs, and the dynamics of sphingolipid—cholesterol microdomainsCurrent Opinion in Cell Biology, 1997
- Equilibrium, Kinetics, Diffusion and Self‐Association of Proteins at Membrane Surfaces: Measurement by Total Internal Reflection Fluorescence MicroscopyPhotochemistry and Photobiology, 1997