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BiP binding keeps ATF6 at bay.

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.[1]


  1. BiP binding keeps ATF6 at bay. Sommer, T., Jarosch, E. Dev. Cell (2002) [Pubmed]
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