Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals

Curr Opin Cell Biol. 2001 Jun;13(3):349-55. doi: 10.1016/s0955-0674(00)00219-2.

Abstract

Cellular survival of endoplasmic reticulum stress requires the unfolded protein response (UPR), a stress response first elucidated genetically in yeast. While we continue to refine our knowledge of the yeast system, especially the breadth and significance of the transcriptional response, conservation of the system's elements has allowed identification of corresponding and additional components of the mammalian UPR. Recent results reveal that the output of the mammalian UPR reaches beyond transcriptional regulation of secretory pathway components to control of general translation, the cell cycle and programmed cell death.

Publication types

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

MeSH terms

  • Animals
  • Apoptosis / physiology
  • Cell Nucleus / metabolism*
  • Endoplasmic Reticulum / metabolism*
  • Endoribonucleases
  • Evolution, Molecular
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • Genetic Variation
  • Humans
  • Mammals / metabolism*
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism
  • Membrane Proteins*
  • Protein Biosynthesis / genetics
  • Protein Biosynthesis / physiology
  • Protein Folding
  • Protein-Serine-Threonine Kinases / genetics
  • Protein-Serine-Threonine Kinases / metabolism*
  • Saccharomyces cerevisiae Proteins*
  • Signal Transduction / physiology*
  • Transcription, Genetic / genetics
  • Transcription, Genetic / physiology
  • Yeasts / metabolism*
  • eIF-2 Kinase / metabolism

Substances

  • Fungal Proteins
  • Membrane Glycoproteins
  • Membrane Proteins
  • Saccharomyces cerevisiae Proteins
  • ERN2 protein, human
  • IRE1 protein, S cerevisiae
  • PERK kinase
  • Protein-Serine-Threonine Kinases
  • eIF-2 Kinase
  • Endoribonucleases