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Keywords:

  • actin turnover;
  • dual-color FRAP;
  • formin homology proteins;
  • s-FDAPplus;
  • single-molecule speckle microscopy

Live-cell single-molecule imaging is a powerful tool to elucidate the in vivo biochemistry of cytoskeletal proteins. However, it is often somewhat difficult to interpret how a bulk population of the observed molecule might behave as a whole. We review our recent studies in which the combination of image analysis with modeling and bulk kinetics measurements such as FRAP (fluorescence recovery after photobleaching) clarified basic problems in the regulation of actin remodeling pathways.