Targeting ERK beyond the boundaries of the kinase active site in melanoma

Mol Carcinog. 2019 Sep;58(9):1551-1570. doi: 10.1002/mc.23047. Epub 2019 Jun 12.

Abstract

Extracellular signal-regulated kinase 1/2 (ERK1/2) constitute a point of convergence for complex signaling events that regulate essential cellular processes, including proliferation and survival. As such, dysregulation of the ERK signaling pathway is prevalent in many cancers. In the case of BRAF-V600E mutant melanoma, ERK inhibition has emerged as a viable clinical approach to abrogate signaling through the ERK pathway, even in cases where MEK and Raf inhibitor treatments fail to induce tumor regression due to resistance mechanisms. Several ERK inhibitors that target the active site of ERK have reached clinical trials, however, many critical ERK interactions occur at other potentially druggable sites on the protein. Here we discuss the role of ERK signaling in cell fate, in driving melanoma, and in resistance mechanisms to current BRAF-V600E melanoma treatments. We explore targeting ERK via a distinct site of protein-protein interaction, known as the D-recruitment site (DRS), as an alternative or supplementary mode of ERK pathway inhibition in BRAF-V600E melanoma. Targeting the DRS with inhibitors in melanoma has the potential to not only disrupt the catalytic apparatus of ERK but also its noncatalytic functions, which have significant impacts on spatiotemporal signaling dynamics and cell fate.

Keywords: D-recruitment site; docking site; protein-protein interaction.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Catalytic Domain / drug effects*
  • Catalytic Domain / genetics
  • Humans
  • MAP Kinase Signaling System / drug effects*
  • Melanoma / drug therapy*
  • Melanoma / genetics
  • Protein Interaction Domains and Motifs / drug effects
  • Protein Kinase Inhibitors / pharmacology*
  • Protein Kinase Inhibitors / therapeutic use*
  • Proto-Oncogene Proteins B-raf / genetics
  • Signal Transduction / drug effects
  • Signal Transduction / genetics

Substances

  • Protein Kinase Inhibitors
  • Proto-Oncogene Proteins B-raf