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. 2019 Jul 22;38(37):6429–6444. doi: 10.1038/s41388-019-0891-6

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© The Author(s) 2019

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — The oncogenic activity of TRIM65 is regulated by phosphorylation. Representative immunoblots of TRIM65 in CRC tissue, matched peritumoral, and normal tissue. T tumor tissue, P peritumor tissue (~2 cm away from tumor), N normal colon or rectal tissue (~5 cm away from the tumor). a Immunoblots of the protein expression of TRIM65 in KM12 cells at different days after transient or stable transfection (days 9 and 15 indicate with puromycin selection) with the TRIM65 overexpression vector. b Representative immunoblots of TRIM65 in KM12 cells treated with CIAP. The TRIM65 isoform (~68 kd) was partially transformed to 57-kd protein when KM12 cells were treated with CIAP phosphatase. c Schematic of the domain structure of TRIM65. TRIM65, consisting of a truly interesting new gene (RING) domain, a B-box domain, and a coiled-coil domain (CC), is followed by distinct C-terminal SPIa and the ryanodine receptor (SPRY) domain; phosphorylation residues S167, S367, and T413 are unambiguously identified, while S166, S172, and S181 are possible ones according to MS/MS peptide mapping. d Analysis of protein expression levels in KM12 cells with transiently ectopic expression of TRIM65 (pLenti-TRIM65) or TRIM65-6A (pCDNA-TRIM65-6A) or TRIM65-6D (pCDNA-TRIM65-6D) compared with the empty control. f Representative images and (l) statistical analysis of wound-healing assays of KM12 cells with transiently ectopic expression of TRIM65 (pLenti-TRIM65) or TRIM65-6A (pCDNA-TRIM65-6A) compared with the empty control. Mean ± S.D., n = 3, ns not significant (p > 0.05), two-tailed Student’s t-test. g Representative images and (m) statistical analysis a wound-healing assays of KM12 cells with transiently ectopic expression of TRIM65 (pLenti-TRIM65) or TRIM65-6D (pCDNA-TRIM65-6D) compared with the empty control. Mean ± S.D., n = 3, ns not significant (p > 0.05), two-tailed Student’s t-test. h Representative images and (j) statistical analysis of invasion assays of KM12 cells with transiently ectopic expression of TRIM65 (pLenti-TRIM65) or TRIM65-6A (pCDNA-TRIM65-6A) compared with the empty control. Mean ± S.D., n = 3, **p < 0.01, *p < 0.05, ns not significant (p > 0.05), two-tailed Student’s t-test. i Representative images and (k) statistical analysis of invasion assays of KM12 cells with transiently ectopic expression of TRIM65 (pLenti-TRIM65) or TRIM65-6D (pCDNA-TRIM65-6D) compared with the empty control. For j, k, l, and m, mean ± S.D., n = 3, ns not significant, two-tailed Student’s t-test