Study on the spatial architecture of p53, MDM2, and p14ARF containing complexes.
We have developed a surface plasmon resonance (SPR)-based immunocapture approach to study multimeric protein-protein complexes. A composition and spatial architecture of protein complexes that contained GST-tagged p53, p14ARF, and MDM2 was examined by the developed approach. Obtained results verified that the p53 protein possesses two binding sites for MDM2. Ternary complexes containing p14ARF, MDM2, and p53 proteins could only be formed when MDM2 protein functions as a bridging molecule. That was confirmed by immunoprecipitation and immunostaining.
Savchenko
Andrej
A
V. Lashkaryov Institute of Semiconductor Physics, NASU, 42 Prospekt Nauki, 03 028 Kyiv, Ukraine.
Yurchenko
Mariya
M
Snopok
Boris
B
Kashuba
Elena
E
D045325:HCT116 Cells; D006801:Humans; D007150:Immunohistochemistry; D008856:Microscopy, Fluorescence; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D051736:Proto-Oncogene Proteins c-mdm2 / Q000737:chemistry* / Q000378:metabolism; D015203:Reproducibility of Results; D012680:Sensitivity and Specificity; D013205:Staphylococcal Protein A / Q000378:metabolism; D020349:Surface Plasmon Resonance; D025803:Tumor Suppressor Protein p14ARF / Q000737:chemistry* / Q000378:metabolism; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000378:metabolism
D046912:Multiprotein Complexes; D013205:Staphylococcal Protein A; D025803:Tumor Suppressor Protein p14ARF; D016159:Tumor Suppressor Protein p53; C497206:MDM2 protein, human; D051736:Proto-Oncogene Proteins c-mdm2