Analysis of the dimerization of human CD99 using bimolecular fluorescence complementation technique.
Two isoforms of human CD99 have been identified, but only heterotypic interaction between the isomers was recently demonstrated. In this study, we performed bimolecular fluorescence complementation analysis to further characterize the interaction in vivo. Upon transiently transfecting plasmids expressing either of the two isoforms fused with yellow fluorescent protein (YFP) fragments, all the YFPtagged CD99 molecules were properly localized on cell surfaces, and formed fluorescent dimers. Interestingly, however, unlike the previous report, the homodimers formed as efficiently as the heterodimer via their extracellular domains, implying its distinct regulatory role through modulating the complex profile.
Lee
Mi-Kyung
MK
Department of Biological Sciences, Konkuk University, Seoul 143-701, Korea.
Kim
Hyun Soo
HS
Kim
Seung-Seok
SS
Cho
Myung-Hwan
MH
Lee
Im-Soon
IS
D000071443:12E7 Antigen; D000595:Amino Acid Sequence; D015703:Antigens, CD / Q000032:analysis* / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D015815:Cell Adhesion Molecules / Q000032:analysis* / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D019281:Dimerization; D005453:Fluorescence; D006801:Humans; D008164:Luminescent Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D020033:Protein Isoforms / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism
D000071443:12E7 Antigen; D015703:Antigens, CD; D001426:Bacterial Proteins; C061828:CD99 protein, human; D015815:Cell Adhesion Molecules; D008164:Luminescent Proteins; D020033:Protein Isoforms; D011993:Recombinant Fusion Proteins; C054562:yellow fluorescent protein, Bacteria