An ATM/TRIM37/NEMO Axis Counteracts Genotoxicity by Activating Nuclear-to-Cytoplasmic NF-κB Signaling

Cancer Res. 2018 Nov 15;78(22):6399-6412. doi: 10.1158/0008-5472.CAN-18-2063. Epub 2018 Sep 25.

Abstract

Blocking genotoxic stress-induced NF-κB activation would substantially enhance the anticancer efficiency of genotoxic chemotherapy. Unlike the well-established classical NF-κB pathway, the genotoxic agents-induced "nuclear-to-cytoplasmic" NF-κB pathway is initiated from the nucleus and transferred to the cytoplasm. However, the mechanism linking nuclear DNA damage signaling to cytoplasmic IKK activation remains unclear. Here, we report that TRIM37, a novel E3 ligase, plays a vital role in genotoxic activation of NF-κB via monoubiquitination of NEMO at K309 in the nucleus, consequently resulting in nuclear export of NEMO and IKK/NF-κB activation. Clinically, TRIM37 levels correlated positively with levels of activated NF-κB and expression of Bcl-xl and XIAP in esophageal cancer specimens, which also associated positively with clinical stage and tumor-node-metastasis classification and associated inversely with overall and relapse-free survival in patients with esophageal cancer. Overexpression of TRIM37 conferred resistance to the DNA-damaging anticancer drug cisplatin in vitro and in vivo through activation of the NF-κB pathway. Genotoxic stress-activated ATM kinase directly interacted with and phosphorylated TRIM37 in the cytoplasm, which induced translocation of TRIM37 into the nucleus, where it formed a complex with NEMO and TRAF6 via a TRAF6-binding motif (TBM). Importantly, blocking the ATM/TRIM37/NEMO axis via cell-penetrating TAT-TBM peptide abrogated genotoxic agent-induced NEMO monoubiquitination and NF-κB activity, resulting in hypersensitivity of cancer cells to genotoxic drugs. Collectively, our results unveil a pivotal role for TRIM37 in genotoxic stress and shed light on mechanisms of inducible chemotherapy resistance in cancer.Significance: In response to genotoxic stress, TRIM37 activates NF-κB signaling via monoubiquitination of NEMO, which subsequently promotes cisplatin chemoresistance and tumor relapse in cancer. Cancer Res; 78(22); 6399-412. ©2018 AACR.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus
  • Animals
  • Antineoplastic Agents / pharmacology
  • Ataxia Telangiectasia Mutated Proteins / metabolism*
  • Cell Nucleus / metabolism*
  • Cisplatin / pharmacology
  • Cytoplasm / metabolism*
  • DNA Damage
  • Drug Resistance, Neoplasm
  • Esophageal Neoplasms / metabolism
  • Female
  • Gene Expression Regulation, Neoplastic
  • Humans
  • I-kappa B Kinase / metabolism*
  • Immunohistochemistry
  • Intracellular Signaling Peptides and Proteins
  • Lymphatic Metastasis
  • Mice
  • Mice, Inbred NOD
  • Mice, Nude
  • Mutagens
  • NF-kappa B p50 Subunit / metabolism*
  • Neoplasm Transplantation
  • Nuclear Proteins / metabolism*
  • Phosphorylation
  • Signal Transduction
  • Stochastic Processes
  • TNF Receptor-Associated Factor 6 / metabolism
  • Tripartite Motif Proteins
  • Ubiquitin-Protein Ligases

Substances

  • Antineoplastic Agents
  • IKBKG protein, human
  • Intracellular Signaling Peptides and Proteins
  • Mutagens
  • NF-kappa B p50 Subunit
  • NFKB1 protein, human
  • Nuclear Proteins
  • TNF Receptor-Associated Factor 6
  • Tifab protein, human
  • Tripartite Motif Proteins
  • TRIM37 protein, human
  • Ubiquitin-Protein Ligases
  • ATM protein, human
  • Ataxia Telangiectasia Mutated Proteins
  • I-kappa B Kinase
  • Cisplatin