F-actin and a type-II myosin are required for efficient clustering of the ER stress sensor Ire1
| Autor: | Kenji Kohno, Ken Takizawa, Yukio Kimata, Yo-hei Yamamoto, Yuki Ishiwata-Kimata |
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| Rok vydání: | 2013 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Physiology RNA Splicing Genes Fungal macromolecular substances Saccharomyces cerevisiae Protein Serine-Threonine Kinases Microtubules Myosin RNA Messenger Cytoskeleton Molecular Biology Actin Membrane Glycoproteins Myosin Heavy Chains Chemistry Endoplasmic reticulum RNA Fungal Cell Biology General Medicine Bridged Bicyclo Compounds Heterocyclic Endoplasmic Reticulum Stress Transmembrane protein Actins Cell biology Repressor Proteins Actin Cytoskeleton Dithiothreitol Basic-Leucine Zipper Transcription Factors Fimbrin Multigene Family RNA splicing Unfolded protein response Thiazolidines Gene Deletion |
| Zdroj: | Cell structure and function. 38(2) |
| ISSN: | 1347-3700 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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