Fluorescence resonance energy transfer (FRET) as a method to calculate the dimerization strength of basic Helix-loop-Helix (bHLH) proteins

Victoria E. Centonze, Beth A. Firulli, Anthony B. Firulli

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Post-translational modifications such as phosphorylation play a vital role in the regulation of protein function. In our study of the basic Helix-loop-Helix (bHLH) transcription factor HAND1, we show that HAND1 is phosphorylated during the trophoblast giant cell differentiation on residues residing in Helix I of the bHLH domain. Our hypothesis is that these modifications result in changes in HAND1 dimerization affinities with other bHLH factors. To test this idea, we employed FRET to measure the protein-protein interactions of HAND1 and HAND1 point mutants in HEK293 cells using YFP and CFP fusion proteins and laser scanning confocal microscopy.

Original languageEnglish (US)
Pages (from-to)78-82
Number of pages5
JournalBiological Procedures Online
Volume6
Issue number1
DOIs
StatePublished - May 12 2004

Keywords

  • Fluorescence resonance energy transfer
  • Phosphorylation
  • Transcription factors

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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