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March 26, 2008Annual Review of BiophysicsOpen Access

Bimolecular Fluorescence Complementation (BiFC) Analysis as a Probe of Protein Interactions in Living Cells

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TKTom K. KerppolaUniversity of Michigan

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Implication

Methodological overview demonstrates bimolecular fluorescence complementation for visualizing protein interactions in living cells, suggesting broad utility across cell types and organisms.

Key Points

To review the principles, applications, and procedural framework of bimolecular fluorescence complementation (BiFC) analysis for directly tracking protein-protein interactions in living cells.
Evaluated the BiFC assay design, which relies on coupling nonfluorescent fragments of a fluorescent reporter to candidate interaction partners.
Assessed compatibility with standard molecular biology protocols, cell culture platforms, regular fluorescence microscopy, and flow cytometry.
Facilitates direct visualization of native intracellular interactions as interacting proteins drive the proximity-dependent reconstitution of a fluorescent complex.
Demonstrates broad qualitative applicability across diverse cell types and whole organisms using conventional laboratory imaging instrumentation.

Cite This Study

Tom K. Kerppola (2008) studied this question.

synapsesocial.com/papers/6a1c07771567d2fc4d5f76b5 https://doi.org/10.1146/annurev.biophys.37.032807.125842

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Implication

Methodological overview demonstrates bimolecular fluorescence complementation for visualizing protein interactions in living cells, suggesting broad utility across cell types and organisms.

Bimolecular Fluorescence Complementation (BiFC) Analysis as a Probe of Protein Interactions in Living Cells

Discussion

Member takes

Implication

Key Points

Cite This Study

Bimolecular Fluorescence Complementation (BiFC) Analysis as a Probe of Protein Interactions in Living Cells

Discussion

Member takes

Implication

Key Points

Cite This Study

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