Endoplasmic reticulum stress in malignancy

Cancer Cell. 2014 May 12;25(5):563-73. doi: 10.1016/j.ccr.2014.03.015.

Abstract

The combination of relative nutrient deprivation and dysregulation of protein synthesis make malignant cells especially prone to protein misfolding. Endoplasmic reticulum stress, which results from protein misfolding within the secretory pathway, has a profound effect on cancer cell proliferation and survival. In this review, we examine the evidence implicating endoplasmic reticulum dysfunction in the pathology of cancer and discuss how recent findings may help to identify novel therapeutic targets.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Activating Transcription Factor 6 / metabolism
  • Antineoplastic Agents / therapeutic use
  • Boronic Acids / therapeutic use
  • Bortezomib
  • Cell Proliferation
  • Cell Survival
  • Endoplasmic Reticulum / metabolism*
  • Endoplasmic Reticulum / pathology
  • Endoplasmic Reticulum Stress / physiology*
  • Endoribonucleases / metabolism
  • Humans
  • Neoplasms / drug therapy
  • Neoplasms / metabolism*
  • Neovascularization, Pathologic
  • Protein Folding*
  • Protein-Serine-Threonine Kinases / metabolism
  • Pyrazines / therapeutic use
  • Unfolded Protein Response
  • eIF-2 Kinase / metabolism

Substances

  • ATF6 protein, human
  • Activating Transcription Factor 6
  • Antineoplastic Agents
  • Boronic Acids
  • Pyrazines
  • Bortezomib
  • EIF2AK3 protein, human
  • ERN1 protein, human
  • Protein-Serine-Threonine Kinases
  • eIF-2 Kinase
  • Endoribonucleases