Sumoylation regulates ER stress response by modulating calreticulin gene expression in XBP-1-dependent mode in Caenorhabditis elegans
- Title
- Sumoylation regulates ER stress response by modulating calreticulin gene expression in XBP-1-dependent mode in Caenorhabditis elegans
- Author
- 안주홍
- Keywords
- Sumoylation; XBP-1; UBC-9; Calreticulin; ER stress; UNFOLDED PROTEIN RESPONSE; ENDOPLASMIC-RETICULUM; OXIDATIVE STRESS; MESSENGER-RNA; SUMO; CALCIUM; DEATH; SMT3; XBP1
- Issue Date
- 2014-06
- Publisher
- PERGAMON-ELSEVIER SCIENCE LTD
- Citation
- The international journal of biochemistry & cell biology, 2014, 53, P.399-408
- Abstract
- Excessive accumulation of unfolded proteins in the endoplasmic reticulum (ER) lumen causes ER stress, which induces a set of genes, including those encoding ER-resident chaperones, to relieve the detrimental effects and recover homeostasis. Calreticulin is a chaperone that facilitates protein folding in the ER lumen, and its gene expression is induced by ER stress in Caenorhabditis elegans. Sumoylation conjugates small ubiquitin-like modifier (SUMO) proteins with target proteins to regulate a variety of biological processes, such as protein stability, nuclear transport, DNA binding, and gene expression. In this study, we showed that C elegans X-box-binding protein 1 (Ce-XBP-1), an ER stress response transcription factor, interacts with the SUMO-conjugating enzyme UBC-9 and a SUMOylation target. Our results indicated that abolishing sumoylation enhanced calreticulin expression in an XBP-1-dependent manner, and the resulting increase in calreticulin counteracted ER stress. Furthermore, sumoylation was repressed in C. elegans undergoing ER stress. Finally, RNAi against ubc-9 mainly affected the expression of genes associated with ER functions, such as lipid and organic acid metabolism. Our results suggest that sumoylation plays a regulatory role in ER function by controlling the expression of genes required for ER homeostasis in C elegans. (C) 2014 Elsevier Ltd. All rights reserved.
- URI
- https://www.sciencedirect.com/science/article/pii/S1357272514002039?via%3Dihub
- ISSN
- 1357-2725
- DOI
- 10.1016/j.biocel.2014.06.005
- Appears in Collections:
- COLLEGE OF NATURAL SCIENCES[S](자연과학대학) > LIFE SCIENCE(생명과학과) > Articles
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