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Related Experiment Video

Updated: May 28, 2026

Bimolecular Fluorescence Complementation
08:54

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

Dimerization of ABCG2 analysed by bimolecular fluorescence complementation.

Ameena J Haider1, Deborah Briggs, Tim J Self

  • 1School of Biomedical Sciences, University of Nottingham, Nottingham, United Kingdom.

Plos One
|October 13, 2011
PubMed
Summary
This summary is machine-generated.

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This study used bimolecular fluorescence complementation to investigate ATP binding cassette transporter ABCG2 dimerization. Results showed specific ABCG2 dimer formation, but single amino acid changes did not alter this dimerization.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • ATP binding cassette transporter ABCG2 exports diverse substrates.
  • ABCG2 activity contributes to multidrug resistance in cancers like leukemia.
  • ABCG2's structure suggests a homodimer is the minimal functional unit.

Purpose of the Study:

  • To investigate ABCG2 dimer formation using bimolecular fluorescence complementation (BiFC).
  • To examine the role of specific amino acid substitutions in ABCG2 dimerization.

Main Methods:

  • ABCG2 was tagged with Venus fluorescent protein (vYFP) fragments without affecting function.
  • Co-expression of tagged ABCG2 allowed detection of dimerization via fluorescence microscopy and flow cytometry.
  • BiFC was employed to analyze specific ABCG2 dimers and the impact of point mutations.

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Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)
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Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)

Published on: June 15, 2018

Determination of Tripartite Interaction between Two Monomers of a MADS-box Transcription Factor and a Calcium Sensor Protein by BiFC-FRET-FLIM Assay
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Determination of Tripartite Interaction between Two Monomers of a MADS-box Transcription Factor and a Calcium Sensor Protein by BiFC-FRET-FLIM Assay

Published on: December 25, 2021

Related Experiment Videos

Last Updated: May 28, 2026

Bimolecular Fluorescence Complementation
08:54

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)
06:45

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)

Published on: June 15, 2018

Determination of Tripartite Interaction between Two Monomers of a MADS-box Transcription Factor and a Calcium Sensor Protein by BiFC-FRET-FLIM Assay
14:34

Determination of Tripartite Interaction between Two Monomers of a MADS-box Transcription Factor and a Calcium Sensor Protein by BiFC-FRET-FLIM Assay

Published on: December 25, 2021

Main Results:

  • BiFC confirmed specific homodimer formation of ABCG2.
  • Tagging ABCG2 with vYFP fragments did not disrupt its cellular trafficking or transport function.
  • Single amino acid substitutions in ABCG2 did not alter dimer formation as detected by BiFC.

Conclusions:

  • ABCG2 forms specific homodimers, a crucial aspect of its function.
  • BiFC is a viable method for studying ABCG2 dimerization.
  • Investigated amino acid substitutions did not significantly impact ABCG2 dimer formation.