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. 2021 Apr 30;12(5):430. doi: 10.1038/s41419-021-03721-9

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© The Author(s) 2021, corrected publication 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 6 — A 293 T cells were transfected with control plasmid and His-GRHL1 plasmid. After serum-free treatment for 12 h and 12 h of stimulation with EGF (100 ng/ml), cells were lysed for immunoprecipitation using an anti-His antibody and blotted with indicated antibodies. B 293 T cells were transfected with His-GRHL1. After serum-free treatment for 12 h and 12 h of stimulation with EGF (100 ng/ml), cells were lysed for immunoprecipitation using anti-ERK1/2 antibody and control rabbit IgG and blotted with indicated antibodies. C A549 cells were transiently transfected with control plasmid, His-GRHL1 plasmid and His-GRHL1(T208A) plasmid respectively. Forty-eight hours later, the cells were lysed. Protein expression was assessed by western blotting using the indicated antibodies. D A549 cells were transfected with His-GRHL1(T208A) plasmid, after serum-free treatment for 12 h and 24 h of stimulation with EGF (100 ng/ml), the nuclear and cytoplasmic fractions were separated and the location of GRHL1 was detected by western blot. E A549 cells were transiently transfected with control plasmid and six mutants (mut1: S25S28S35A, mut2: S76S77A, mut3: S95A, mut4: S442A, mut5: S493S501A, mut6: S539A) plasmids respectively. Forty-eight hours later, the cells were lysed. Protein expression was assessed by western blotting using the indicated antibodies. F A549 cells were transfected with His-GRHL1 plasmid and His-GRHL1(S76S77A) plasmid, after serum-free treatment for 12 h and 24 h of stimulation with EGF (100 ng/ml), the nuclear and cytoplasmic fractions were separated and the GRHL1 in nuclear was detected by western blot. G A549 cells were transiently transfected with control plasmid, His-GRHL1(S76A), and His-GRHL1(S77A) plasmids respectively. Forty-eight hours later, the cells were lysed. Protein expression was assessed by western blotting using the indicated antibodies. H A549 cells were transfected with His-GRHL1 plasmid and His-GRHL1(S76A) plasmid, after serum-free treatment for 12 h and 24 h of stimulation with EGF (100 ng/ml), the nuclear and cytoplasmic fractions were separated and the location of GRHL1 was detected by western blot. I–J A549 and H1299 cells were transfected with His-GRHL1 plasmid and His-GRHL1(S76A) plasmid. After serum-free treatment for 12 h, EGF (100 ng/ml) was added. After 12 h. The location of GRHL1 was detected by immunofluorescence staining. Cells were stained with anti-GRHL1 (left panel, red) and DAPI (middle panel, blue). The merged images are shown in the right panel. Scale bar = 25 µm, magnification: ×400.