Article
Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response.
Molecular and cellular biology - 1 Feb 2005
Shen Jingshi, Snapp Erik L, Lippincott-Schwartz Jennifer, Prywes Ron
Abstract excerpt
Endoplasmic reticulum (ER) stress-induced activation of ATF6, an ER membrane-bound transcription factor, requires a dissociation step from its inhibitory regulator, BiP. It has been generally postulated that dissociation of the BiP-ATF6 complex is a result of the competitive binding of misfolded proteins generated during ER stress. Here we present evidence against this model and for an active regulatory mechanism...
Topics
- Activating Transcription Factor 6
- Adenosine Triphosphate
- Animals
- COS Cells
- Chlorocebus aethiops
- DNA-Binding Proteins
- Dithiothreitol
- Endoplasmic Reticulum
- Endoplasmic Reticulum Chaperone BiP
- HeLa Cells
- Heat-Shock Proteins
- Humans
- Mice
- Molecular Chaperones