Abstract
The unfolded protein response (UPR) is fundamental for development and adaption in eukaryotic cells. Arabidopsis has become one of the best model systems to uncover conserved mechanisms of the UPR in multicellular eukaryotes as well as organism-specific regulation of the UPR in plants. Monitoring the UPR in planta is an elemental approach to identifying regulatory components and to revealing molecular mechanisms of the plant UPR. In this chapter, we provide protocols for the induction and analyses of plant UPR at a molecular level in Arabidopsis. Three kinds of ER stress treatment methods and quantitation of the plant UPR activation are described here.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Kozutsumi Y, Segal M, Normington K, Gething MJ, Sambrook J (1988) The presence of malfolded proteins in the endoplasmic-reticulum signals the induction of glucose-regulated proteins. Nature 332:462–464
Back SH, Schroder M, Lee K, Zhang KZ, Kaufman RJ (2005) ER stress signaling by regulated splicing: IRE1/HAC1/XBP1. Methods 35:395–416
Takatsuk A, Arima K, Tamura G (1971) Tunicamycin, a new antibiotic.1. Isolation and characterization of tunicamycin. J Antibiot 24:215–223
Heifetz A, Keenan RW, Elbein AD (1979) Mechanism of action of tunicamycin on the UDP-GlcNAC-dolichyl-phosphate GlcNAC-1-phosphate transferase. Biochemistry 18:2186–2192
Keller RK, Boon DY, Crum FC (1979) N-acetylglucosamine-1-phosphate transferase from hen oviduct—solubilization, characterization, and inhibition by tunicamycin. Biochemistry 18:3946–3952
Brandish PE, Kimura K, Inukai M, Southgate R, Lonsdale JT, Bugg TDH (1996) Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli. Antimicrob Agents Chemother 40:1640–1644
Acosta-Alvear D, Zhou Y, Blais A, Tsikitis M, Lents NH, Arias C, Lennon CJ, Kluger Y, Dynlacht BD (2007) XBP1 controls diverse cell type- and condition-specific transcriptional regulatory networks. Mol Cell 27:53–66
Cox JS, Walter P (1996) A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87:391–404
Iwata Y, Koizumi N (2005) An Arabidopsis transcription factor, AtbZIP60, regulates the endoplasmic reticulum stress response in a manner unique to plants. Proc Natl Acad Sci U S A 102:5280–5285
Lu DP, Christopher DA (2008) Endoplasmic reticulum stress activates the expression of a sub-group of protein disulfide isomerase genes and AtbZIP60 modulates the response in Arabidopsis thaliana. Mol Genet Genomics 280:199–210
Chen YN, Brandizzi F (2012) AtIRE1A/AtIRE1B and AGB1 independently control two essential unfolded protein response pathways in Arabidopsis. Plant J 69:266–277
Acknowledgments
This study was supported by grants from the National Institutes of Health (R01 GM101038-01), Chemical Sciences, Geosciences and Biosciences Division, Office of Basic Energy Sciences, Office of Science, U.S. DOE (DE-FG02-91ER20021), NASA (NNX12AN71G) and the National Science Foundation (MCB 0948584 and MCB1243792).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 Springer Science+Business Media, LLC
About this protocol
Cite this protocol
Chen, Y., Brandizzi, F. (2013). Analysis of Unfolded Protein Response in Arabidopsis. In: Running, M. (eds) G Protein-Coupled Receptor Signaling in Plants. Methods in Molecular Biology, vol 1043. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-532-3_8
Download citation
DOI: https://doi.org/10.1007/978-1-62703-532-3_8
Published:
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-62703-531-6
Online ISBN: 978-1-62703-532-3
eBook Packages: Springer Protocols