CIN85 interacts with PHD2. CIN85 interacts with PHD2. A, Endogenous PHD2 was immunoprecipitated (IP) with CIN85 antibody from MDA-MB-231, BT-549, and Hs.

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CIN85 interacts with PHD2. CIN85 interacts with PHD2. A, Endogenous PHD2 was immunoprecipitated (IP) with CIN85 antibody from MDA-MB-231, BT-549, and Hs 578T cells and probed for PHD2 and CIN85. Blots from the input were probed with PHD1, -2, -3, CIN85, HIF1α, and HIF2α antibody. B, Western blot analysis of immunoprecipitates and inputs from HEK-293 cells expressing V5-tagged PHD1, PHD2, or PHD3 and Myc-tagged CIN85. Blots from immunoprecipitates were probed with V5-tag antibody; the input was probed with V5-tag, Myc-tag, and α-tubulin antibodies. C, Schematic presentation of BiFC assay constructs. The constructs CMV-CIN85-YN and CMV-PHD2-YC allow expression of CIN85 and PHD2 as fusion proteins with the N-terminal or the C-terminal nonfluorescent parts of YFP (-YN and -YC) under the control of the CMV promoter, respectively. Note that CMV-YN and CMV-YC protein parts are nonfluorescent and noninteracting; however, interacting proteins such as CIN85 and PHD2 are able to reconstitute fluorescent YFP. D, Visualization of the BiFC signal by confocal microscopy in BT-549 cells expressing CMV-CIN85-YN + CMV-PHD2-YC. No signal was detected upon expression of CMV-YN + CMV-YC. Scale bar, 20 μm. E, The surface plasmon resonance sensorgram of CIN85 binding to immobilized PHD2. Binding was assessed upon injection of a concentration series of CIN85 over immobilized PHD2. The CIN85 concentrations were 0, 10, 21, 42, 84, 168, 337, 675, 1,350, and 2,700 nmol/L (from bottom to top). F, The fitted curve for different concentrations of CIN85 binding to immobilized PHD2 using the “Affinity” model in the Biacore T200 evaluation software. Nina Kozlova et al. Cancer Res 2019;79:4042-4056 ©2019 by American Association for Cancer Research