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.
MeSH terms
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Activating Transcription Factor 6
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Animals
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Carrier Proteins / metabolism*
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DNA-Binding Proteins / metabolism*
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Endoplasmic Reticulum / metabolism*
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Endoplasmic Reticulum / ultrastructure
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Endoplasmic Reticulum Chaperone BiP
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Eukaryotic Cells / metabolism*
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Eukaryotic Cells / ultrastructure
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Golgi Apparatus / metabolism*
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Golgi Apparatus / ultrastructure
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Heat-Shock Proteins*
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Humans
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Molecular Chaperones / metabolism*
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Protein Binding / physiology
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Protein Folding*
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Signal Transduction / physiology
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Transcription Factors / metabolism*
Substances
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ATF6 protein, human
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Activating Transcription Factor 6
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Carrier Proteins
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DNA-Binding Proteins
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Endoplasmic Reticulum Chaperone BiP
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Heat-Shock Proteins
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Molecular Chaperones
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Transcription Factors