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.
Max-Delbrück Center for Molecular Medicine, Robert-Rossle Str. 10, D-13092, Berlin, Germany.
Thomas
T
Sommer
Ernst
E
Jarosch
D051702:Activating Transcription Factor 6; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism* / Q000648:ultrastructure; D000091342:Endoplasmic Reticulum Chaperone BiP; D005057:Eukaryotic Cells / Q000378:metabolism* / Q000648:ultrastructure; D006056:Golgi Apparatus / Q000378:metabolism* / Q000648:ultrastructure; D006360:Heat-Shock Proteins; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology; D017510:Protein Folding; D015398:Signal Transduction / Q000502:physiology; D014157:Transcription Factors / Q000378:metabolism*
C497111:ATF6 protein, human; D051702:Activating Transcription Factor 6; D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D014157:Transcription Factors