A CK2 and SUMO-Dependent, PML NB-Involved Regulatory Mechanism Controlling BLM Ubiquitination and G-Quadruplex Resolution

Authors

Shichang Liu
Erin Atkinson
Adriana Paulucci-Holthauzen
Bin Wang

Publication Date

9-30-2023

Journal

Nature Communications

DOI

10.1038/s41467-023-41705-9

PMID

37777511

PMCID

PMC10542384

PubMedCentral® Posted Date

9-30-2023

PubMedCentral® Full Text Version

Post-print

Abstract

The Boom syndrome helicase (BLM) unwinds a variety of DNA structures such as Guanine (G)-quadruplex. Here we reveal a role of RNF111/Arkadia and its paralog ARKL1, as well as Promyelocytic Leukemia Nuclear Bodies (PML NBs), in the regulation of ubiquitination and control of BLM protein levels. RNF111 exhibits a non-canonical SUMO targeted E3 ligase (STUBL) activity targeting BLM ubiquitination in PML NBs. ARKL1 promotes RNF111 localization to PML NBs through SUMO-interacting motif (SIM) interaction with SUMOylated RNF111, which is regulated by casein kinase 2 (CK2) phosphorylation of ARKL1 at a serine residue near the ARKL1 SIM domain. Upregulated BLM in ARKL1 or RNF111-deficient cells leads to a decrease of G-quadruplex levels in the nucleus. These results demonstrate that a CK2- and RNF111-ARKL1-dependent regulation of BLM in PML NBs plays a critical role in controlling BLM protein levels for the regulation of G-quadruplex.

Keywords

Humans, Casein Kinase II, Promyelocytic Leukemia Nuclear Bodies, Promyelocytic Leukemia Protein, RecQ Helicases, Ubiquitination, Sumoylation, SUMO-1 Protein

Comments

This article has been corrected. See Nat Commun. 2024 Feb 5;15:1077.

Published Open-Access

yes

Recommended Citation

Liu, Shichang; Atkinson, Erin; Paulucci-Holthauzen, Adriana; et al., "A CK2 and SUMO-Dependent, PML NB-Involved Regulatory Mechanism Controlling BLM Ubiquitination and G-Quadruplex Resolution" (2023). Faculty, Staff and Student Publications. 5115.
https://digitalcommons.library.tmc.edu/uthgsbs_docs/5115