BiP binding keeps ATF6 at bay.

Thomas Sommer; Ernst Jarosch

doi:10.1016/s1534-5807(02)00210-1

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PubMed · 12110159

BiP binding keeps ATF6 at bay.

Thomas Sommer·Ernst Jarosch

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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.

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Activating Transcription Factor 6 Animals Carrier Proteins DNA-Binding Proteins Endoplasmic Reticulum Endoplasmic Reticulum Chaperone BiP Eukaryotic Cells Golgi Apparatus Heat-Shock Proteins Humans Molecular Chaperones Protein Binding Protein Folding Signal Transduction Transcription Factors Journal Article Review Comment

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Thomas Sommer, Ernst Jarosch. 2002. BiP binding keeps ATF6 at bay.. https://doi.org/10.1016/s1534-5807(02)00210-1

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