Cargando…

Oncogenic β-catenin mutations evade pH-regulated degradation

β-catenin has roles in cell-cell adhesion and Wnt signaling. We recently showed that β-catenin protein abundance is decreased at higher intracellular pH (pHi), mediated by pH-sensitive interaction with the beta-transducin repeat containing E3 ubiquitin protein ligase (β-TrCP). Increased pHi facilita...

Descripción completa

Detalles Bibliográficos
Autores principales: Grillo-Hill, Bree K., White, Katharine A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6370367/
https://www.ncbi.nlm.nih.gov/pubmed/30788422
http://dx.doi.org/10.1080/23723556.2018.1554470
_version_ 1783394356563017728
author Grillo-Hill, Bree K.
White, Katharine A.
author_facet Grillo-Hill, Bree K.
White, Katharine A.
author_sort Grillo-Hill, Bree K.
collection PubMed
description β-catenin has roles in cell-cell adhesion and Wnt signaling. We recently showed that β-catenin protein abundance is decreased at higher intracellular pH (pHi), mediated by pH-sensitive interaction with the beta-transducin repeat containing E3 ubiquitin protein ligase (β-TrCP). Increased pHi facilitates β-TrCP binding and degradation of β-catenin. β-catenin mutations that abrogate the pH-sensitive interaction induce significant tumors not seen with other β-catenin stabilizing mutants.
format Online
Article
Text
id pubmed-6370367
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher Taylor & Francis
record_format MEDLINE/PubMed
spelling pubmed-63703672020-01-02 Oncogenic β-catenin mutations evade pH-regulated degradation Grillo-Hill, Bree K. White, Katharine A. Mol Cell Oncol Author’s Views β-catenin has roles in cell-cell adhesion and Wnt signaling. We recently showed that β-catenin protein abundance is decreased at higher intracellular pH (pHi), mediated by pH-sensitive interaction with the beta-transducin repeat containing E3 ubiquitin protein ligase (β-TrCP). Increased pHi facilitates β-TrCP binding and degradation of β-catenin. β-catenin mutations that abrogate the pH-sensitive interaction induce significant tumors not seen with other β-catenin stabilizing mutants. Taylor & Francis 2019-01-02 /pmc/articles/PMC6370367/ /pubmed/30788422 http://dx.doi.org/10.1080/23723556.2018.1554470 Text en © 2018 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.
spellingShingle Author’s Views
Grillo-Hill, Bree K.
White, Katharine A.
Oncogenic β-catenin mutations evade pH-regulated degradation
title Oncogenic β-catenin mutations evade pH-regulated degradation
title_full Oncogenic β-catenin mutations evade pH-regulated degradation
title_fullStr Oncogenic β-catenin mutations evade pH-regulated degradation
title_full_unstemmed Oncogenic β-catenin mutations evade pH-regulated degradation
title_short Oncogenic β-catenin mutations evade pH-regulated degradation
title_sort oncogenic β-catenin mutations evade ph-regulated degradation
topic Author’s Views
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6370367/
https://www.ncbi.nlm.nih.gov/pubmed/30788422
http://dx.doi.org/10.1080/23723556.2018.1554470
work_keys_str_mv AT grillohillbreek oncogenicbcateninmutationsevadephregulateddegradation
AT whitekatharinea oncogenicbcateninmutationsevadephregulateddegradation