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. 2024 Jun 11;15:4969. doi: 10.1038/s41467-024-49221-0

Fig. 5. Nuclear MYG1 recruits HSP90 to phosphorylate PKM2 and increase its stability.

Fig. 5

a Representative images of the co-localization of MYG1 and PKM2 in 293 T, HCT116, and SW480 cells (left, scale bar, 10 μm), and Pearson’s correlation coefficient (PCC) was analyzed in the ROI marked with dashed lines. 293 T and HCT116 cells were treated with EGF (100 ng/mL) for 10 h before fixing. Representative of 24 images from n = 3 independent experiments (left), and each point represents the average PCC of each experiment (right). 293 T (b) and HCT116 (d) cells were treated with EGF (100 ng/mL) for 10 h and lysed for immunoprecipitation. 293 T (c) and LoVo (e) cells were treated with EGF (100 ng/mL) for 10 h and lysed for immunoprecipitation. f 293 T cells treated with EGF (100 ng/mL) for 10 h were fractioned into cytosol and nucleus and then subjected to immunoprecipitation. g 293 T cells transfected with different MYG1 constructs were treated with EGF (100 ng/mL) for 10 h and lysed for immunoprecipitation. h SW480 and HCT116 cells expressing MYG1 variants were detected for PKM2 protein level. i MYG1 KO LoVo cells treated with CHX (50 μg/mL) were harvested at 0, 2, 4, 6 h followed by detecting MYG1 and PKM2 protein levels by western blot (left) and quantified (right). j–m 293 T and LoVo cells treated as indicated were collected to detect the interaction of MYG1 with HSP90 (j), PKM2 with HSP90 (k), MYG1 with GSK3β (l), and PKM2 with GSK3β (m). n HCT116 cells transfected with MYG1 or MYG1∆ treated with EGF (100 ng/mL) or GSK3 inhibitor IX (10 μM) for 10 h were subjected to immunoprecipitation. o LoVo cells transfected with siRNAs of HSP90 (#1, #2) were treated and detected as in n. n = 3 independent experiments (b–o). See also Supplementary Fig. 6. Source data are provided as a Source Data file.