F-actin and a Type-II myosin are required for efficient clustering of the ER stress sensor Ire1

Cell Structure and Function

Volumn 38, Issue 2, 2013, Pages 135-143

  Ishiwata Kimata, Yuki ^a   Yamamoto, Yo Hei ^a   Takizawa, Ken ^a   Kohno, Kenji ^a   Kimata, Yukio ^a  

^a NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

Cytoskeleton; Molecular chaperone; Organelle; Stress response; UPR

Indexed keywords

F ACTIN; LATRUNCULIN A; MYOSIN II; PROTEIN IRE1;

ACTIN FILAMENT; ARTICLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM STRESS; FUNGAL GENE; GENE CLUSTER; GENE DELETION; GENE FUNCTION; GENE LOCATION; MYO1 GENE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; RNA SPLICING; SAC6 GENE; YEAST CELL;

ACTIN CYTOSKELETON; ACTINS; BASIC-LEUCINE ZIPPER TRANSCRIPTION FACTORS; BICYCLO COMPOUNDS, HETEROCYCLIC; DITHIOTHREITOL; ENDOPLASMIC RETICULUM STRESS; GENE DELETION; GENES, FUNGAL; MEMBRANE GLYCOPROTEINS; MICROTUBULES; MULTIGENE FAMILY; MYOSIN HEAVY CHAINS; PROTEIN-SERINE-THREONINE KINASES; REPRESSOR PROTEINS; RNA SPLICING; RNA, FUNGAL; RNA, MESSENGER; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; THIAZOLIDINES;

EID: 84879747327     PISSN: 03867196     EISSN: 13473700     Source Type: Journal    
DOI: 10.1247/csf.12033     Document Type: Article

References (22)

1. Adams, A.E., Botstein, D., and Drubin, D.G. 1991. Requirement of yeast fimbrin for actin organization and morphogenesis in vivo. Nature, 354: 404-408.
2. Aragon, T., van Anken, E., Pincus, D., Serafimova, I.M., Korennykh, A.V., Rubio, C.A., and Walter, P. 2009. Messenger RNA targeting to endoplasmic reticulum stress signalling sites. Nature, 457: 736-740.
3. Credle, J.J., Finer-Moore, J.S., Papa, F.R., Stroud, R.M., and Walter, P. 2005. On the mechanism of sensing unfolded protein in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA, 102: 18773-18784.
4. Estrada, P., Kim, J., Coleman, J., Walker, L., Dunn, B., Takizawa, P., Novick, P., and Ferro-Novick, S. 2003. Myo4p and She3p are required for cortical ER inheritance in Saccharomyces cerevisiae. J. Cell Biol., 163: 1255-1266.
5. Fehrenbacher, K.L., Davis, D., Wu, M., Boldogh, I., and Pon, L.A. 2002. Endoplasmic reticulum dynamics, inheritance, and cytoskeletal interactions in budding yeast. Mol. Biol. Cell, 13: 854-865.
6. Gardner, B.M. and Walter, P. 2011. Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response. Science, 333: 1891-1894.
7. He, Y., Beatty, A., Han, X., Ji, Y., Ma, X., Adelstein, R.S., Yates, J.R., Kemphues, K., and Qi, L. 2012. Nonmuscle Myosin IIB Links Cytoskeleton to IRE1α Signaling during ER Stress. Dev. Cell, 23: 1141-1152.
8. Kimata, Y., Kimata, Y.I., Shimizu, Y., Abe, H., Farcasanu, I.C., Takeuchi, M., Rose, M.D., and Kohno, K. 2003. Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins. Mol. Biol. Cell, 14: 2559-2569.
9. Kimata, Y., Oikawa, D., Shimizu, Y., Ishiwata-Kimata, Y., and Kohno, K. 2004. A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1. J. Cell Biol., 167: 445-456.
10. Kimata, Y., Ishiwata-Kimata, Y., Ito, T., Hirata, A., Suzuki, T., Oikawa, D., Takeuchi, M., and Kohno, K. 2007. Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins. J. Cell Biol., 179: 75-86.
11. Kimata, Y. and Kohno, K. 2011. Endoplasmic reticulum stress-sensing mechanisms in yeast and mammalian cells. Curr. Opin. Cell Biol., 23: 135-142.
12. Korennykh, A.V., Egea, P.F., Korostelev, A.A., Finer-Moore, J., Zhang, C., Shokat, K.M., Stroud, R.M., and Walter, P. 2009. The unfolded protein response signals through high-order assembly of Ire1. Nature, 457: 687-693.
13. Li, H., Korennykh, A.V., Behrman, S.L., and Walter, P. 2010. Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering. Proc. Natl. Acad. Sci. USA, 107: 16113-16118.
14. Merksamer, P.I., Trusina, A., and Papa, F.R. 2008. Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions. Cell, 135: 933-947.
15. Mori, K., Kawahara, T., Yoshida, H., Yanagi, H., and Yura, T. 1996. Signalling from endoplasmic reticulum to nucleus: transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway. Genes Cells, 1: 803-817.
16. Mori, K. 2009. Signalling pathways in the unfolded protein response: development from yeast to mammals. J. Biochem., 146: 743-750.
17. Oikawa, D., Kimata, Y., and Kohno, K. 2007. Self-association and BiP dissociation are not sufficient for activation of the ER stress sensor Ire1. J. Cell Sci., 120: 1681-1688.
18. Prinz, W.A., Grzyb, L., Veenhuis, M., Kahana, J.A., Silver, P.A., and Rapoport, T.A. 2000. Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae. J. Cell Biol., 150: 461-474.
19. Promlek, T., Ishiwata-Kimata, Y., Shido, M., Sakuramoto, M., Kohno, K., and Kimata, Y. 2011. Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways. Mol. Biol. Cell, 22: 3520-3532.
20. Ron, D. and Walter, P. 2007. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol., 8: 519-529.
21. Ueda, H., Yokota, E., Kutsuna, N., Shimada, T., Tamura, K., Shimmen, T., Hasezawa, S., Dolja, V.V., and Hara-Nishimura, I. 2010. Myosin-dependent endoplasmic reticulum motility and F-actin organization in plant cells. Proc. Natl. Acad. Sci. USA, 107: 6894-6899.
22. Wagner, W., Brenowitz, S.D., and Hammer, J.A., 3rd, 2011. Myosin-Va transports the endoplasmic reticulum into the dendritic spines of Purkinje neurons. Nat. Cell Biol., 13: 40-48.