Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2021 Jun 21;40:200. doi: 10.1186/s13046-021-01994-8

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 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.

PMC Copyright notice

Fig. 4 — IMP3 directly binds to MEKK1 and activates MEK/ERK pathway. (A) Flow chart of bioinformatics analysis predicting candidate RNAs regulated by IMP3. (B) MAPK cascades were enriched in IMP3 regulated targets. (C) RIP assay showing that MEKK1 interacted with IMP3 in RKO cells. The RT-qPCR products were analyzed by electrophoresis (below) (*p < 0.05), CD44 was used as a positive control. (D) The schematic diagram of IMP3 potential binding site in MEKK1 UTR area. E-F. Luciferase reporter assay, (E1)293T cell was transfected with IMP3, (E2) RKO cell was transfected with IMP3 siRNAs, (F)LOVO cell was co-transfected with IMP3 and MEKK1 3’UTR wt and indicated mutations. The luciferase assay data were normalized to firefly luciferase activity. (*p < 0.05). (G)GEPIA analyzed the expression of IMP3 and MEKK1 in CRC tissues. (H) Representative images of IHC staining of IMP3 and MEKK1 in the colon tissues from Villin-Cre IMP3^−/− and IMP3^fl/fl mice treated with AOM/DSS. (I) The mRNA level of MEKK1 in indicated cells (* p < 0.05). (J) The protein level of MEKK1 and its downstream pathways in indicated cells. MEK1: mitogen-activated protein kinase kinase 1; ERK: extracellular-signal-regulated kinase; JNK: c-Jun N-terminal kinase; MAPK: mitogen-activated protein kinase; The prefix p represents its phosphorylation. (K) RT-qPCR analysis of MEKK1 mRNA stability in actinomycin D treated CRC cells (* p < 0.05). (L) CCK-8 results showed that knockdown of MEKK1 or using MEK/ERK inhibitor U0126 attenuated the enhanced cell viability induced by overexpression of IMP3 in LOVO cells (* p < 0.05). Representative images of (M) wound healing assays and (N) transwell assays showed that MEKK1 repression or U0126 rescued the enhanced invasion and migration ability by overexpression of IMP3 (* p < 0.05)