Toward quantitative "in vivo biochemistry" with fluorescence fluctuation spectroscopy

Quantitative description of protein dynamics and interactions in vivo with temporal and spatial resolution is a key step in dissecting molecular mechanisms in cell biology. Fluorescence fluctuation spectroscopy (FFS) has recently emerged as a powerful in vivo tool for assessing molecular concentrati...

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Bibliographic Details
Published in:Molecular biology of the cell 2010-12, Vol.21 (24), p.4306-4311
Main Authors: Slaughter, Brian D, Li, Rong
Format: Article
Language:English
Subjects:
Algorithms
Animals
Cells, Cultured
Diffusion
Drosophila
Fungal Proteins - chemistry
Fungal Proteins - metabolism
Humans
MBoC Technical
Protein Interaction Mapping - methods
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Tertiary
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - metabolism
Spectrometry, Fluorescence - methods
Time Factors
Yeasts - chemistry
Yeasts - metabolism
Zebrafish
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Summary:Quantitative description of protein dynamics and interactions in vivo with temporal and spatial resolution is a key step in dissecting molecular mechanisms in cell biology. Fluorescence fluctuation spectroscopy (FFS) has recently emerged as a powerful in vivo tool for assessing molecular concentration and movement and formation of hetero- and homo-oligomeric complexes. This article discusses point FFS-based analysis methods that have proven useful to cell biologists, focusing on the kinds of information they provide, their pros and cons, and the basic instrumentation required. Along the way, we describe briefly a few recent examples where these analyses have helped address important biological questions.
ISSN:1059-1524
1939-4586
DOI:10.1091/mbc.E10-05-0451