Fluorescence fluctuation spectroscopy and imaging methods for examination of dynamic protein interactions in yeast

Brian D. Slaughter, Jay R. Unruh, Rong Li

Research output: Chapter in Book/Report/Conference proceedingChapter

9 Scopus citations

Abstract

Protein interactions are inherently dynamic. In no system is this more true and important than in signaling pathways, where spatial and temporal control of specific protein interactions is key to signaling specificity and timing. While genetic and biochemical interactions form a necessary and important starting point for deciphering interactions among signaling components, they struggle to provide precise information of where and when interactions occur in a live cell setting. In contrast, live cell fluorescence studies such as those outlined below are able to provide quantitative information on the strength, nature, timing, and location of homotypic and heterotypic protein interactions.

Original languageEnglish (US)
Title of host publicationYeast Systems Biology
Subtitle of host publicationMethods and Protocols
EditorsJuan I. Castrillo, Stephen G. Oliver
Pages283-306
Number of pages24
DOIs
StatePublished - Oct 24 2011
Externally publishedYes

Publication series

NameMethods in Molecular Biology
Volume759
ISSN (Print)1064-3745

Keywords

  • 2D PCH
  • Fluorescence fluctuation spectroscopy (FFS)
  • fluorescence correlation spectroscopy (FCS)
  • fluorescence cross-correlation spectroscopy (FCCS)
  • fluorescence resonance energy transfer (FRET)
  • number and brightness analysis (N&B)
  • photon counting histogram (PCH)
  • signaling pathway

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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