Fig. 4: Acetylation affected the subcellular localization of SRPK1. | Communications Biology

Fig. 4: Acetylation affected the subcellular localization of SRPK1.

From: SRPK1 acetylation modulates alternative splicing to regulate cisplatin resistance in breast cancer cells

Fig. 4

a MCF7 and MCF7R cells were treated with cisplatin for 5 days and immunostained for SRPK1. The nuclei were counterstained with Hoechst 33342. Scale bar: 20 µm. b, c 231 and 231R cells were treated with cisplatin and the potential interaction between SRPK1 and HSP90 was characterized by co-immunoprecipitation assays using the indicated antibodies. d HeLa cells were transfected with GFP-tagged SRPK1 or Mut7. The subcellular localization of GFP signals was examined by the fluorescence microscopy. Scale bar: 5 µm. Bars: mean ± SD; n = 4; **p < 0.01 by Student’s t-test. e HeLa cells overexpressing Myc-tagged SRPK1 or Mut7 were fractionated. The relative abundance of Myc-SRPK1 and phosphorylated SRSFs in the cytoplasm (Cy) and nucleus (Nu) was determined by immunoblotting. GAPDH was used as a cytoplasmic marker. LaminA and CLK1 were markers for the nuclear fraction. Cisp: cisplatin. The immunofluorescence images in (a) are representative of four experiments with similar results. The Western blots in (b, c, e) are representative of three experiments with similar results.

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