2007年3月
Cellular response to unfolded proteins in the endoplasmic reticulum of plants
FEBS JOURNAL
- 巻
- 274
- 号
- 5
- 開始ページ
- 1152
- 終了ページ
- 1171
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1111/j.1742-4658.2007.05664.x
- 出版者・発行元
- BLACKWELL PUBLISHING
Secretory and transmembrane proteins are synthesized in the endoplasmic reticulum (ER) in eukaryotic cells. Nascent polypeptide chains, which are translated on the rough ER, are translocated to the ER lumen and folded into their native conformation. When protein folding is inhibited because of mutations or unbalanced ratios of subunits of hetero-oligomeric proteins, unfolded or misfolded proteins accumulate in the ER in an event called ER stress. As ER stress often disturbs normal cellular functions, signal-transduction pathways are activated in an attempt to maintain the homeostasis of the ER. These pathways are collectively referred to as the unfolded protein response (UPR). There have been great advances in our understanding of the molecular mechanisms underlying the UPR in yeast and mammals over the past two decades. In plants, a UPR analogous to those in yeast and mammals has been recognized and has recently attracted considerable attention. This review will summarize recent advances in the plant UPR and highlight the remaining questions that have yet to be addressed.
- リンク情報
- ID情報
-
- DOI : 10.1111/j.1742-4658.2007.05664.x
- ISSN : 1742-464X
- PubMed ID : 17257164
- Web of Science ID : WOS:000244111100005