BiP binding keeps ATF6 at bay

Dev Cell. 2002 Jul;3(1):1-2. doi: 10.1016/s1534-5807(02)00210-1.

Abstract

A study by, in this issue of Developmental Cell shows that transport to the Golgi complex and subsequent proteolytic activation of the stress-regulated transcription factor ATF6 is initiated by the dissociation of the ER chaperone BiP from ATF6. This demonstrates that BiP is a key element in sensing the folding capacity within the ER and provides mechanistic insights on how the activation of membrane-bound transcription factors can be regulated.

Publication types

  • Review
  • Comment

MeSH terms

  • Activating Transcription Factor 6
  • Animals
  • Carrier Proteins / metabolism*
  • DNA-Binding Proteins / metabolism*
  • Endoplasmic Reticulum / metabolism*
  • Endoplasmic Reticulum / ultrastructure
  • Endoplasmic Reticulum Chaperone BiP
  • Eukaryotic Cells / metabolism*
  • Eukaryotic Cells / ultrastructure
  • Golgi Apparatus / metabolism*
  • Golgi Apparatus / ultrastructure
  • Heat-Shock Proteins*
  • Humans
  • Molecular Chaperones / metabolism*
  • Protein Binding / physiology
  • Protein Folding*
  • Signal Transduction / physiology
  • Transcription Factors / metabolism*

Substances

  • ATF6 protein, human
  • Activating Transcription Factor 6
  • Carrier Proteins
  • DNA-Binding Proteins
  • Endoplasmic Reticulum Chaperone BiP
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Transcription Factors