Introduction
ER Stress and the Environment
Abiotic stresses brought about by drought, heat, freezing, or saline conditions result in some of the greatest crop losses worldwide. The frequency of adverse conditions due to climate change presents serious challenges to global agriculture, which already suffers annual crop losses estimated at billions of dollars (Mittler and Blumwald 2010). Therefore, there is great interest in understanding how plants respond to stress and in endowing crop plants with traits for stress tolerance.
This chapter deals with a type of plant stress called endoplasmic reticulum (ER) stress. In learning about what plant cells do, the ER is sometimes overlooked – the focus is usually on chloroplasts, mitochondria, nuclei, or cell walls. Nonetheless, the ER is important in stress management because the ER senses abiotic and biotic stresses and responds to them.
The ER plays a key role in many cellular activities because, among other things, the ER is the gateway...
References
Aebi M, Bernasconi R, Clerc S, Molinari M. N-glycan structures: recognition and processing in the ER. Trends Biochem Sci. 2010;35:74–82.
Anelli T, Sitia R. Protein quality control in the early secretory pathway. EMBO J. 2008;27:315–27.
Braakman I, Bulleid NJ. Protein folding and modification in the mammalian endoplasmic reticulum. Annu Rev Biochem. 2011;80:71–99.
Brodsky JL, Wojcikiewicz RJ. Substrate-specific mediators of ER associated degradation (ERAD). Curr Opin Cell Biol. 2009;21:1–6.
Brown MS, Ye J, Rawson RB, Goldstein JL. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell. 2000;100:391–8.
Caramelo JJ, Parodi AJ. Getting in and out from calnexin/calreticulin cycles. J Biol Chem. 2008;283:10221–5.
Caro LG, Palade GE. Protein synthesis, storage, and discharge in the pancreatic exocrine cell. An autoradiographic study. J Cell Biol. 1964;20:473–95.
Christianson JC, Olzmann JA, Shaler TA, Sowa ME, Bennett EJ, Richter CM, Tyler RE, Greenblatt EJ, Harper JW, Kopito RR. Defining human ERAD networks through an integrative mapping strategy. Nat Cell Biol. 2012;14:93–105.
Di Cola A, Frigerio L, Lord JM, Roberts LM, Ceriotti A. Endoplasmic reticulum-associated degradation of ricin A chain has unique and plant-specific features. Plant Physiol. 2005;137:287–96.
Gething MJ. Role and regulation of the ER chaperone BiP. Semin Cell Dev Biol. 1999;10:465–72.
Hammond C, Helenius A. Folding of VSV G protein: sequential interaction with BiP and calnexin. Science. 1994;266:456–8.
Hebert DN, Bernasconi R, Molinari M. ERAD substrates: which way out? Semin Cell Dev Biol. 2010;21:526–32.
Hong Z, Li J. The protein quality control of plant receptor-like kinases in the endoplasmic reticulum. In: Tax F, Kemmerling B, editors. Receptor-like Kinases in Plants. Berlin: Springer; 2012. p. 275–307.
Howell SH. ER stress responses in plants. Annu Rev Plant Biol. 2013;64:477–99.
Initiative TA. Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature. 2000;408:796–815.
Jurgens G. Membrane trafficking in plants. Annu Rev Cell Dev Biol. 2004;20:481–504.
Keenan RJ, Freymann DM, Stroud RM, Walter P. The signal recognition particle. Annu Rev Biochem. 2001;70:755–75.
Kornfeld R, Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem. 1985;54:631–64.
Liu Y, Bassham DC. Autophagy: pathways for self-eating in plant cells. Annu Rev Plant Biol. 2011;63:215–37.
Lupattelli F, Pedrazzini E, Bollini R, Vitale A, Ceriotti A. The rate of phaseolin assembly Is controlled by the glucosylation state of Its N-linked oligosaccharide chains. Plant Cell. 1997;9:597–609.
Mittler R, Blumwald E. Genetic engineering for modern agriculture: challenges and perspectives. Annu Rev Plant Biol. 2010;61:443–62.
Mori K. Signalling pathways in the unfolded protein response: development from yeast to mammals. J Biochem. 2009;146:743–50.
Ruddock LW, Molinari M. N-glycan processing in ER quality control. J Cell Sci. 2006;119:4373–80.
Shao S, Hegde RS. Membrane protein insertion at the endoplasmic reticulum. Annu Rev Cell Dev Biol. 2011;27:25–56.
Totani K, Ihara Y, Tsujimoto T, Matsuo I, Ito Y. The recognition motif of the glycoprotein-folding sensor enzyme UDP-Glc:glycoprotein glucosyltransferase. Biochemistry. 2009;48:2933–40.
Vierstra RD. The expanding universe of ubiquitin and ubiquitin-like modifiers. Plant Physiol. 2012;160(1):2–14.
Walter P. Walking along the serendipitous path of discovery. Mol Biol Cell. 2010;21:15–7.
Walter P, Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science. 2011;334:1081–6.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2014 Springer Science+Business Media New York
About this entry
Cite this entry
Howell, S. (2014). Cytoplasm: ER Stress. In: Howell, S. (eds) Molecular Biology. Springer, New York, NY. https://doi.org/10.1007/978-1-4939-0263-7_9-1
Download citation
DOI: https://doi.org/10.1007/978-1-4939-0263-7_9-1
Received:
Accepted:
Published:
Publisher Name: Springer, New York, NY
Online ISBN: 978-1-4939-0263-7
eBook Packages: Springer Reference Biomedicine and Life SciencesReference Module Biomedical and Life Sciences