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BiP binding keeps ATF6 at bay

Item Type:Editorial
Title:BiP binding keeps ATF6 at bay
Creators Name:Sommer, T. and Jarosch, E.
Abstract:A study by Shen et al. 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.
Keywords:Activating Transcription Factor 6, Carrier Proteins, DNA-Binding Proteins, Endoplasmic Reticulum, Eukaryotic Cells, Golgi Apparatus, Heat-Shock Proteins, Molecular Chaperones, Protein Binding, Protein Folding, Signal Transduction, Transcription Factors, Animals
Source:Developmental Cell
Publisher:Cell Press
Page Range:1-2
Date:11 July 2002
Official Publication:https://doi.org/10.1016/S1534-5807(02)00210-1
PubMed:View item in PubMed

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