Multiple E3 ligases control tankyrase stability and function.


Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
08 11 2023
Historique:
received: 22 05 2023
accepted: 26 10 2023
medline: 9 11 2023
pubmed: 8 11 2023
entrez: 8 11 2023
Statut: epublish

Résumé

Tankyrase 1 and 2 are ADP-ribosyltransferases that catalyze formation of polyADP-Ribose (PAR) onto themselves and their binding partners. Tankyrase protein levels are regulated by the PAR-binding E3 ligase RNF146, which promotes K48-linked polyubiquitylation and proteasomal degradation of tankyrase and its partners. We identified a novel interaction between tankyrase and a distinct class of E3 ligases: the RING-UIM (Ubiquitin-Interacting Motif) family. We show that RNF114 and RNF166 bind and stabilize monoubiquitylated tankyrase and promote K11-linked diubiquitylation. This action competes with RNF146-mediated degradation, leading to stabilization of tankyrase and its binding partner, Angiomotin, a cancer cell signaling protein. Moreover, we identify multiple PAR-binding E3 ligases that promote ubiquitylation of tankyrase and induce stabilization or degradation. Discovery of K11 ubiquitylation that opposes degradation, along with identification of multiple PAR-binding E3 ligases that ubiquitylate tankyrase, provide insights into mechanisms of tankyrase regulation and may offer additional uses for tankyrase inhibitors in cancer therapy.

Identifiants

pubmed: 37938264
doi: 10.1038/s41467-023-42939-3
pii: 10.1038/s41467-023-42939-3
pmc: PMC10632493
doi:

Substances chimiques

Ubiquitin-Protein Ligases EC 2.3.2.27
Tankyrases EC 2.4.2.30
ADP Ribose Transferases EC 2.4.2.-
Ribose 681HV46001

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

7208

Subventions

Organisme : NIH HHS
ID : S10 OD010582
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA016087
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM141292
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM129780
Pays : United States

Commentaires et corrections

Type : UpdateOf

Informations de copyright

© 2023. The Author(s).

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Auteurs

Jerome Perrard (J)

Department of Cell Biology, New York University School of Medicine, New York, NY, 10016, USA.

Susan Smith (S)

Department of Cell Biology, New York University School of Medicine, New York, NY, 10016, USA. susan.smith@med.nyu.edu.

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Classifications MeSH