2013年
F-actin and a Type-II Myosin Are Required for Efficient Clustering of the ER Stress Sensor Ire1
CELL STRUCTURE AND FUNCTION
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- 巻
- 38
- 号
- 2
- 開始ページ
- 135
- 終了ページ
- 143
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1247/csf.12033
- 出版者・発行元
- JAPAN SOC CELL BIOLOGY
Endoplasmic reticulum (ER) stress causes the ER-resident transmembrane protein Ire1 to self-associate, leading to the formation of large oligomeric clusters. In yeast cells, this induces strong unfolded protein response (UPR) through splicing of HAC1 mRNA. Here, we demonstrate that highly ER-stressed yeast cells exhibited poor Ire1 clustering in the presence of the actin-disrupting agent latrunculin-A. Under these conditions, Ire1 may form smaller oligomers because latrunculin-A only partially diminished the Ire1-mediated splicing of HAC1 mRNA. Ire1 cluster formation was also impaired by deletion of the type-II myosin gene MYO1 or SAC6, which encodes the actin-bundling protein fimbrin. Finally, we demonstrated that Ire1 clusters are predominantly located on or near actin filaments. Therefore, we propose that actin filaments play an important role in ER stress-induced clustering of Ire1.
- リンク情報
- ID情報
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- DOI : 10.1247/csf.12033
- ISSN : 0386-7196
- eISSN : 1347-3700
- PubMed ID : 23666407
- Web of Science ID : WOS:000329105200001