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 Jan 15;12:383. doi: 10.1038/s41467-020-20669-0

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

© The Author(s) 2021

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/.

PMC Copyright notice

Fig. 4 — a TAp63 and ΔNp63 isoforms domains: TA transactivation domain, DBD DNA-binding domain, OD oligomerization domain, SAM sterile alpha motif, TID transactivation inhibitory domain. The C-terminus of p63β and p63γ diverge from p63α starting from residue 411 or 512, respectively. b The relative luciferase activity expressed as the fold over control (Ctr) of TAp63 isoforms shows that specific C-terminus amino acids do not reduce transcriptional activity except the TID in case of the α-isoform. TAp63 (..572) misses the post-SAM part of the protein; TAp63 (…411) reflect the common part of TAp63β; and TAp63γ with TAp63α. n = 3 biologically independent experiments, luciferase assay was performed in triplicates on PUMA 4xBS2WT responsive elements (REs). Data are presented as mean ± SD, p-value by two-tailed unpaired Student’s t-test. WB analysis of TAp63 isoforms and deletion variants in luciferase assay extracts are shown below the graph. GAPDH was used as loading control; c Oligomeric state analysis of the indicated p63 isoforms via BN-PAGE expressed in vitro in rabbit reticulocyte lysate. The oligomeric conformation is indicated by T (tetramer), D (dimer), M (monomer); d The relative luciferase activity expressed as fold over control (Ctr) shows the ability of TAp63α and β to transactivate the PUMA and NOXA promoters. n = 3 biologically independent experiments, luciferase assay was performed in triplicates. Data are presented as mean ± SD, p-value by two-tailed unpaired Student’s t-test; e The relative luciferase activity expressed as the fold over control (Ctr) shows the ability of ΔNp63α and ΔNp63β to transactivate the Envoplakin (ENV) and Bullous pemphigoid antigen 1 (BPAG1) promoters. n = 3 biologically independent experiments, luciferase assay was performed in triplicates. Data are presented as mean ± SD, p-value by two-tailed unpaired Student’s t-test. Source data are provided as a Source Data file.