How IRE1 reacts to ER stress

Cell. 2008 Jan 11;132(1):24-6. doi: 10.1016/j.cell.2007.12.017.

Abstract

The long-awaited structure of the effector portion of IRE1, the endoplasmic reticulum stress transducer, is published in this issue of Cell (Lee et al., 2008). This structure provides new insight into the mysterious coupling of kinase and endoribonuclease activities in the oldest, most-conserved branch of the unfolded protein response in eukaryotes.

Publication types

  • Comment
  • Review

MeSH terms

  • Alternative Splicing / physiology
  • Catalytic Domain / physiology
  • Endoplasmic Reticulum / metabolism*
  • Endoplasmic Reticulum / ultrastructure
  • Endoribonucleases / chemistry
  • Endoribonucleases / genetics
  • Endoribonucleases / metabolism
  • Membrane Glycoproteins / chemistry*
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism
  • Oxidative Stress / physiology*
  • Phosphotransferases / chemistry
  • Phosphotransferases / genetics
  • Phosphotransferases / metabolism
  • Protein Structure, Tertiary / physiology
  • Protein-Serine-Threonine Kinases / chemistry*
  • Protein-Serine-Threonine Kinases / genetics
  • Protein-Serine-Threonine Kinases / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Yeasts / metabolism*
  • Yeasts / ultrastructure

Substances

  • Membrane Glycoproteins
  • Saccharomyces cerevisiae Proteins
  • Phosphotransferases
  • IRE1 protein, S cerevisiae
  • Protein-Serine-Threonine Kinases
  • Endoribonucleases