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. 2021 Feb 18;40:75. doi: 10.1186/s13046-021-01877-y

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© The Author(s) 2021

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 6 — PP1α activity is decreased in CAC tissues and correlates with SRSF1-dependent MKNK2 alternative splicing. a There was no statistical difference of PPP1CA mRNA levels between tumor tissues and adjacent nontumorous tissues. P value was based on paired Student’s t-test (n = 32). b Representative IHC images showed the immunoreactivities of total PP1α and phosphorylated-PP1α (pT320-PP1α) in clinical specimens. Scale bar: 100 μm. c Although no difference regarding total PP1α protein level was observed between tumor and adjacent tissues (left panel), tumor tissues exhibited higher phosphorylation on T320 site (pT320-PP1α, right panel) based on IHC data. P value was based on paired Student’s t-test (n = 32). d Tumor tissues with higher nucleus SRSF1 showed higher pT320-PP1α levels. P value was based on unpaired Student’s t-test. e Spearman correlation test further confirmed a positive correlation between nucleus SRSF1 and pT320-PP1α levels. f Spearman correlation test identified a negative correlation between pT320-PP1α and MKNK2a levels. In contrast, MKNK2b was positively correlated with pT320-PP1α level. g Proliferation capacity of SW480 cells or HCT-116 cells (h) was impaired by overexpressing pcDNA-PP1α-T320A, a constitutively active PP1α construct, as revealed by MTT assays. P value was based on unpaired Student’s t-test. i Colony formation assay was conducted for the cells described in (g) and (h), further indicating that PP1α-T320A may attenuate CAC proliferation. j CAC cells were transfected with three different PP1α constructs, including PP1α-WT, PP1α-T320A (constitutively active mutant), and PP1α-H125A (kinase-dead mutant) using pcDNA-vector as control. The levels of phosphorylated SRSF1, nucleus SRSF1 were measured by western blotting, and the MKNK2 splicing were evaluated by RT-PCR (lower panel). Semi-quantification of immunoblotting results and corresponding RT-qPCR data were shown in Supplementary Figure S8D. (K) CAC cells were transfected with PP1α-WT or PP1α-T320A with/without tautomycetin treatment. The levels of phosphorylated SRSF1, nucleus SRSF1 were measured by western blotting, and MKNK2 splicing were evaluated by RT-PCR (lower panel). Semi-quantification of immunoblotting results and corresponding RT-qPCR data were shown in Supplementary Figure S8E