Visualization of interactions among bZip and Rel family proteins in living cells using bimolecular fluorescence complementation

被引:1234
作者
Hu, CD
Chinenov, Y
Kerppola, TK [1 ]
机构
[1] Univ Michigan, Sch Med, Howard Hughes Med Inst, Ann Arbor, MI 48109 USA
[2] Univ Michigan, Sch Med, Dept Biol Chem, Ann Arbor, MI 48109 USA
关键词
D O I
10.1016/S1097-2765(02)00496-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Networks of protein interactions coordinate cellular functions. We describe a bimolecular fluorescence complementation (BiFC) assay for determination of the locations of protein interactions in living cells. This approach is based on complementation between two nonfluorescent fragments of the yellow fluorescent protein (YFP) when they are brought together by interactions between proteins fused to each fragment. BiFC analysis was used to investigate interactions among bZIP and Rel family transcription factors. Regions outside the bZIP domains determined the locations of bZIP protein interactions. The subcellular sites of protein interactions were regulated by signaling. Cross-family interactions between bZIP and Rel proteins affected their subcellular localization and modulated transcription activation. These results attest to the general applicability of the BiFC assay for studies of protein interactions.
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页码:789 / 798
页数:10
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