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Updated: Jul 6, 2026
Bimolecular Fluorescence Complementation
Published on: April 15, 2011
Analysis of the dimerization of human CD99 using bimolecular fluorescence complementation technique
Mi-Kyung Lee1, Hyun Soo Kim, Seung-Seok Kim
1Department of Biological Sciences, Konkuk University, Seoul 143-701, Korea.
Human CD99 protein has two forms that interact. This study shows CD99 homodimers form as readily as heterodimers, suggesting a new regulatory role for CD99 in cell signaling.
Area of Science:
- Molecular Biology
- Cell Biology
- Immunology
Background:
- Two isoforms of human CD99 exist.
- Previous research demonstrated heterotypic interactions between CD99 isoforms.
Purpose of the Study:
- To investigate CD99 isoform interactions in vivo.
- To characterize homodimer and heterodimer formation of CD99.
Main Methods:
- Bimolecular fluorescence complementation (BiFC) analysis.
- Transient transfection of cells with plasmids encoding YFP-tagged CD99 isoforms.
- Confocal microscopy to visualize YFP fluorescence and protein localization.
Main Results:
- YFP-tagged CD99 isoforms localized to the cell surface.
- Both homodimers and heterodimers of CD99 isoforms were formed.
- Homodimer formation was as efficient as heterodimer formation.
Conclusions:
- CD99 isoforms can form homodimers and heterodimers via their extracellular domains.
- Homodimerization of CD99 may play a distinct regulatory role.
- Modulation of CD99 complex formation influences cellular functions.
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