A CK2 and SUMO-dependent, PML NB-involved regulatory mechanism controlling BLM ubiquitination and G-quadruplex resolution

Shichang Liu, Erin Atkinson, Adriana Paulucci-Holthauzen and Bin Wang ()
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Shichang Liu: The University of Texas M.D. Anderson Cancer Center
Erin Atkinson: The University of Texas M.D. Anderson Cancer Center
Adriana Paulucci-Holthauzen: The University of Texas M.D. Anderson Cancer Center
Bin Wang: The University of Texas M.D. Anderson Cancer Center

Nature Communications, 2023, vol. 14, issue 1, 1-15

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-41705-9

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