Dishevelled-1 DIX and PDZ domain lysine residues regulate oncogenic Wnt signaling.
chromatin immunoprecipitation (ChIP)
dishevelled (DVL)
gene expression
lysine residue
post-translational modification
Journal
Oncotarget
ISSN: 1949-2553
Titre abrégé: Oncotarget
Pays: United States
ID NLM: 101532965
Informations de publication
Date de publication:
26 Oct 2021
26 Oct 2021
Historique:
received:
03
08
2021
accepted:
24
09
2021
entrez:
4
11
2021
pubmed:
5
11
2021
medline:
5
11
2021
Statut:
epublish
Résumé
DVL proteins are central mediators of the Wnt pathway and relay complex input signals into different branches of the Wnt signaling network. However, molecular mechanism(s) that regulate DVL-mediated relay of Wnt signals still remains unclear. Here, for the first time, we elucidate the functional significance of three DVL-1 lysines (K/Lys) which are subject to post-translational acetylation. We demonstrate that K34 Lys residue in the DIX domain regulates subcellular localization of β-catenin, thereby influencing downstream Wnt target gene expression. Additionally, we show that K69 (DIX domain) and K285 (PDZ domain) regulate binding of DVL-1 to Wnt target gene promoters and modulate expression of Wnt target genes including
Identifiants
pubmed: 34733415
doi: 10.18632/oncotarget.28089
pii: 28089
pmc: PMC8555683
doi:
Types de publication
Journal Article
Langues
eng
Pagination
2234-2251Subventions
Organisme : NCI NIH HHS
ID : R01 CA155223
Pays : United States
Informations de copyright
Copyright: © 2021 Sharma et al.
Déclaration de conflit d'intérêts
CONFLICTS OF INTEREST Authors have no conflicts of interest to declare.
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