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

Author

Listed:
  • Shichang Liu

    (The University of Texas M.D. Anderson Cancer Center)

  • Erin Atkinson

    (The University of Texas M.D. Anderson Cancer Center
    The MD Anderson Cancer Center and UT Health Graduate School of Biomedical Sciences)

  • Adriana Paulucci-Holthauzen

    (The University of Texas M.D. Anderson Cancer Center)

  • Bin Wang

    (The University of Texas M.D. Anderson Cancer Center
    The MD Anderson Cancer Center and UT Health Graduate School of Biomedical Sciences)

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.

Suggested Citation

  • Shichang Liu & Erin Atkinson & Adriana Paulucci-Holthauzen & Bin Wang, 2023. "A CK2 and SUMO-dependent, PML NB-involved regulatory mechanism controlling BLM ubiquitination and G-quadruplex resolution," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-41705-9
    DOI: 10.1038/s41467-023-41705-9
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    References listed on IDEAS

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    1. Annie M. Sriramachandran & Katrin Meyer-Teschendorf & Stefan Pabst & Helle D. Ulrich & Niels H. Gehring & Kay Hofmann & Gerrit J. K. Praefcke & R. Jürgen Dohmen, 2019. "Arkadia/RNF111 is a SUMO-targeted ubiquitin ligase with preference for substrates marked with SUMO1-capped SUMO2/3 chain," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
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