BiP binding keeps ATF6 at bay

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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
ISSN:	1534-5807
Publisher:	Cell Press
Volume:	3
Number:	1
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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