4.8 Article

AtIRE1A/AtIRE1B and AGB1 independently control two essential unfolded protein response pathways in Arabidopsis

Journal

PLANT JOURNAL
Volume 69, Issue 2, Pages 266-277

Publisher

WILEY-BLACKWELL
DOI: 10.1111/j.1365-313X.2011.04788.x

Keywords

unfolded protein response; inositol-requiring enzyme 1; GTP-binding protein ss 1; endoplasmic reticulum stress; root; Arabidopsis thaliana

Categories

Funding

  1. Chemical Sciences, Geosciences and Biosciences Division, Office of Basic Energy Sciences, Office of Science, US Department of Energy [DE-FG02-91ER20021]
  2. National Aeronautics and Space Agency [NNH08ZTT003N NRA-08-FSB_Prop-0052]

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The endoplasmic reticulum (ER) has the ability to maintain the balance between demand for and synthesis of secretory proteins. To ensure protein-folding homeostasis in the ER, cells invoke signaling pathways known as the unfolded protein response (UPR). To initiate UPR, yeasts largely rely on a conserved sensor, IRE1. In metazoans, there are at least three independent UPR signalling pathways. Some UPR transducers have been identified in plants, but no genetic interaction among them has yet been examined. The Arabidopsis genome encodes two IRE1 sequence homologs, AtIRE1A and AtIRE1B. Here we provide evidence that AtIRE1A and AtIRE1B have overlapping functions that are essential for the plant UPR. A double mutant of AtIRE1A and AtIRE1B, atire1a atire1b, showed reduced ER stress tolerance and a compromised UPR activation phenotype. We have also established that Arabidopsis AGB1, a subunit of the ubiquitous heterotrimeric GTP-binding protein family, and AtIRE1A/AtIRE1B independently control two essential plant UPR pathways. By demonstrating that atire1a atire1b has a short root phenotype that is enhanced by an agb1 loss-of-function mutation, we have identified a role for UPR transducers in organ growth regulation.

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