Fig. 4: The protein stability of dCK was regulated by HSP90 via ubiquitin-proteasome pathway in HeLa cells. | Cell Death Discovery

Fig. 4: The protein stability of dCK was regulated by HSP90 via ubiquitin-proteasome pathway in HeLa cells.

From: HSP90 regulates dCK stability and inhibits ionizing radiation-induced ferroptosis in cervical cancer cells

Fig. 4

A Scatter plots for TCGA data’s HSP90AA1 and dCK correlation analysis. B 17-AAG lowered the levels of dCK and endogenous HSP90 protein. C Western blot analysis in HeLa cells overexpressing HSP90. D HeLa cells transfected with sh-Control, sh-HSP90#1, sh-HSP90#2, and sh-HSP90#3 were subjected to Western blot analysis. E, F Analysis was done on the endogenous dCK protein half-life that decreased by 17-AAG after cycloheximide (CHX) treatment. G, H HeLa cells were treated with 10 µM MG-132 and 30 μM CQ to prevent proteasomal degradation and autophagosome-lysosome fusion. I Western blotting was used to evaluate the expression of dCK in HeLa cells following either si-NEDD4L alone or in combination with 17-AAG. J, K The analysis of the experiment’s half-life of the endogenous NEDD4L protein was conducted after 48 h of transfection with Myc-HSP90 plasmids, and the sample was treated with cycloheximide (CHX) for 4 6, 8, 12 h. L In HeLa cells, the input and ubiquitin IP samples were subjected to Western blot analysis using the designated antibody. M, N Western blot analysis of NEDD4L and dCK protein level. O The interaction between WWP1/2 and NEDD4L, dCK or HSP90.

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