Journal
JOURNAL OF BIOCHEMISTRY
Volume 149, Issue 5, Pages 507-518Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvr041
Keywords
bZIP transcription factor; endoplasmic reticulum stress; OASIS family; regulated intramembrane proteolysis; unfolded protein response
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Funding
- Japan Society for the Promotion of Science KAKENHI [22020030, 22800049]
- Sumitomo Foundation
- Kanae Foundation for the Promotion of medical Science
- Mitsui Sumitomo Insurance Welfare Foundation
- Japan Health Foundation
- Suzuken Memorial Foundation
- Uehara Memorial Foundation
- Takeda Science foundation
- Astellas Foundation for Research on Metabolic Disorders
- Grants-in-Aid for Scientific Research [22020030, 22800049] Funding Source: KAKEN
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Eukaryotic cells can adapt to endoplasmic reticulum (ER) dysfunction by producing diverse signals from the ER to the cytosol or nucleus. These signalling pathways are collectively known as the unfolded protein response (UPR). The canonical branches of the UPR are mediated by three ER membrane-bound proteins: PERK, IRE1 and ATF6. These ER stress transducers basically play important roles in cell survival after ER stress. Recently, novel types of ER stress transducers that share a region of high sequence similarity with ATF6 have been identified. They have a transmembrane domain, which allows them to associate with the ER, and possess a transcription-activation domain and a bZIP domain. These membrane-bound bZIP transcription factors include Luman, OASIS, BBF2H7, CREBH and CREB4. Despite their structural similarities with ATF6, differences in activating stimuli, tissue distribution and response element binding indicate specialized functions of each member on regulating the UPR in specific organs and tissues. Here, we summarize our current understanding of the biochemical characteristics and physiological functions of the ER-resident bZIP transcription factors.
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