Interference with ERK-dimerization at the nucleocytosolic interface targets pathological ERK1/2 signaling without cardiotoxic side-effects

Nat Commun. 2020 Apr 7;11(1):1733. doi: 10.1038/s41467-020-15505-4.

Abstract

Dysregulation of extracellular signal-regulated kinases (ERK1/2) is linked to several diseases including heart failure, genetic syndromes and cancer. Inhibition of ERK1/2, however, can cause severe cardiac side-effects, precluding its wide therapeutic application. ERKT188-autophosphorylation was identified to cause pathological cardiac hypertrophy. Here we report that interference with ERK-dimerization, a prerequisite for ERKT188-phosphorylation, minimizes cardiac hypertrophy without inducing cardiac adverse effects: an ERK-dimerization inhibitory peptide (EDI) prevents ERKT188-phosphorylation, nuclear ERK1/2-signaling and cardiomyocyte hypertrophy, protecting from pressure-overload-induced heart failure in mice whilst preserving ERK1/2-activity and cytosolic survival signaling. We also examine this alternative ERK1/2-targeting strategy in cancer: indeed, ERKT188-phosphorylation is strongly upregulated in cancer and EDI efficiently suppresses cancer cell proliferation without causing cardiotoxicity. This powerful cardio-safe strategy of interfering with ERK-dimerization thus combats pathological ERK1/2-signaling in heart and cancer, and may potentially expand therapeutic options for ERK1/2-related diseases, such as heart failure and genetic syndromes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cardiotoxicity*
  • Cell Culture Techniques
  • Cell-Penetrating Peptides / chemical synthesis
  • Cell-Penetrating Peptides / pharmacology*
  • Cell-Penetrating Peptides / toxicity
  • Colonic Neoplasms / drug therapy
  • Colonic Neoplasms / metabolism
  • Dimerization*
  • Drug Delivery Systems
  • Extracellular Signal-Regulated MAP Kinases / drug effects
  • Extracellular Signal-Regulated MAP Kinases / metabolism*
  • Heart Failure / drug therapy
  • Heart Failure / metabolism
  • Humans
  • Lung Neoplasms / drug therapy
  • Lung Neoplasms / metabolism
  • MAP Kinase Signaling System* / drug effects
  • MAP Kinase Signaling System* / physiology
  • Mice
  • Mice, Inbred C57BL
  • Molecular Medicine
  • Rats
  • Rats, Sprague-Dawley
  • Signal Transduction

Substances

  • Cell-Penetrating Peptides
  • penetratin
  • Extracellular Signal-Regulated MAP Kinases