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E-GEOD-124235

ABSTRACT: BLISTER safeguards the protein kinase activity of ER stress modulator IRE1A during plant growth and development in Arabidopsis thaliana

PROVIDER: E-GEOD-124235 | ExpressionAtlas | 2020-04-17

REPOSITORIES: ExpressionAtlas

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			Action	DRS
	E-GEOD-124235-analysis-methods.tsv	Tabular
	E-GEOD-124235-analytics.tsv	Tabular
	E-GEOD-124235-atlasExperimentSummary.Rdata	Rdata
	E-GEOD-124235-configuration.xml	Xml
	E-GEOD-124235-g4_g1-mvaPlot.png	Other

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BLISTER safeguards the protein kinase activity of ER stress modulator IRE1A during plant growth and development in Arabidopsis thaliana

Project description:BLISTER safeguards the protein kinase activity of ER stress modulator IRE1A during plant growth and development in Arabidopsis thaliana

| PRJNA511129 | ENA

A functional unfolded protein response is required for normal vegetative development in Arabidopsis

Project description:The Unfolded Protein Response (UPR) is activated in plants in response to ER stress and plays an important role in mitigating stress damage. We have analyzed an ire1a ire1b bzip17 triple mutant in Arabidopsis with defects in stress signaling and found that the mutant is also impaired in vegetative plant growth under conditions without externally applied stress. This raises the question as to whether the UPR functions in plant development in same manner as it does in responding to stress. bZIP17 is an ER-associated membrane transcription factor that is mobilized to the nucleus in response to stress. Through the analysis of a mobilization defective bZIP17 mutant, we found that bZIP17 must be capable of mobilization to support normal plant development. Likewise, through the analysis of ire1 mutants, we found that protein kinase and ribonuclease activities of IRE1 must be functional to support normal development. These findings demonstrate that the UPR is active, albeit at low levels, during unstressed conditions, and that these activities are required for normal development.

2019-04-17 | GSE120672 | GEO

BLISTER safeguards the protein kinase activity of ER stress modulator IRE1A during plant growth and development in Arabidopsis thaliana

Project description:BLI tightly controls the protein kinase activity of IRE1A in plants,and IRE1A plays new roles in plant growth and development

2019-11-01 | GSE124235 | GEO

Photorespiratory stress in catalase deficient plants

Project description:Hydrogen peroxide (H2O2) can act as a signaling molecule that influences various aspects of plant growth and development, including stress signaling and cell death. To unravel the molecular mechanisms that regulate the response towards an impact of increased H2O2 levels in plant cells, we focused on the photorespiration-dependent peroxisomal H2O2 production in Arabidopsis thaliana mutants lacking CATALASE2 (CAT2) activity (cat2-2).

2016-06-10 | GSE77171 | GEO

Photorespiratory stress in catalase deficient plants

2016-06-10 | E-GEOD-77171 | biostudies-arrayexpress

Neurons shift translational control to secure proteostatic resilience during ER stress

Project description:Proteostasis is essential for survival and particularly important for highly specialized post mitotic cells like neurons. Transient reduction of protein synthesis by protein kinase R–like endoplasmic reticulum (ER) kinase (PERK)-mediated phosphorylation of eukaryotic translation initiation factor 2α (eIF2α) is a major proteostatic survival response during ER stress. Paradoxically, neurons are remarkably tolerant to PERK dysfunction, which suggests the existence of cell type-specific mechanisms that secure proteostatic stress resilience. We employed PERK-deficient neuron and astrocyte monocultures to investigate the mechanisms underlying neuron-specific ER stress resilience in the absence of PERK.

2022-06-13 | GSE200742 | GEO

Control of Translation during the Unfolded Protein Response in Maize seedlings: Life without PERKs.

Project description:The accumulation of misfolded proteins in the endoplasmic reticulum (ER) defines a condition called ER stress that induces the unfolded protein response (UPR). The UPR in mammalian cells attenuates protein synthesis initiation, which prevents the piling up of misfolded proteins in the ER. Mammalian cells rely on Protein Kinase RNA-Like Endoplasmic Reticulum Kinase (PERK) phosphorylation of eIF2alpha to arrest protein synthesis, however, plants do not have a PERK homolog, so the question is whether plants control translation in response to ER stress. We compared changes in RNA levels in the transcriptome to the RNA levels protected by ribosomes and found a decline in translation efficiency, including many UPR genes, in response to ER stress. The decline in translation efficiency is due to the fact that many mRNAs are not loaded onto polyribosomes (polysomes) in proportion to their increase in total RNA, instead some of the transcripts accumulate in stress granules (SGs). The RNAs that populate SGs are not derived from the disassembly of polysomes because protein synthesis remains steady during stress. Thus, the surge in transcription of UPR genes in response to ER stress is accompanied by the formation of SGs, and the sequestration of mRNAs in SGs may serve to temporarily relieve the translation load during ER stress.

2020-07-08 | GSE153969 | GEO

A novel positive feed-back loop mediated by the membrane-associated transcription factor NTL3 is important for heat stress tolerance in rice

Project description:Global warming has great impacts on plant growth and development. Heat shock transcription factors are the master regulators of heat stress response to alleviate protein misfolding in the cytosol in plants. However, how plants deal with accumulation of misfolded proteins in the endoplasmic reticulum (ER) under heat stress conditions is less understood, especially in crops such as in rice. Here we report a positive feed-back loop mediated by the membrane-associated transcription factors NTL3 and bZIP74 in heat stress response in rice. In response to heat stress, the ER-membrane-associated bZIP74 is activated and up-regulate the expression of NTL3 in rice; NTL3 encodes an ER-membrane-associated transcription factor that is activated and regulate downstream genes including bZIP74 involved in protein folding and reactive oxygen species scavenging. Loss-of-function mutations of NTL3 are sensitive to heat stress while inducible expression of the processed form of NTL3 increases heat stress tolerance in rice seedlings. Our work reveals the important role of NTL3 in ER stress response for heat stress tolerance in rice.

2020-04-20 | GSE122021 | GEO

ATP-Competitive Partial Antagonists—'PAIR's—Segregate IRE1α’s RNase-Mediated Biological Outputs

Project description:During mammalian cell growth and differentiation, the unfolded protein response (UPR) homeostatically adjusts endoplasmic reticulum (ER) protein-folding capacity to match changing cellular secretory demands. However, under high/chronic ER stress conditions the UPR triggers apoptosis. This dichotomy is promoted in part by differential activation levels of the ER transmembrane kinase/endoribonuclease (RNase) IRE1a. IRE1a kinase auto-phosphorylation operates as a rheostat to control downstream RNase-induced outputs that either sustain adaptive ER protein-folding or cause apoptosis. We have previously shown that IRE1a’s RNase activity can be activated or fully inactivated by ATP-competitive kinase inhibitors. Here we developed a new class of ATP-competitive kinase inhibitors that partially antagonize the RNase of IRE1a at full occupancy. An atomic level resolution co-crystal structure shows that these small molecule partial antagonists—which we named ‘PAIR’s for (Partial Antagonists of IRE1a RNase)—occupy the ATP-binding site of IRE1a and partially displace a helix (helix aC) in the kinase domain that forms part of a dimeric interface. In insulin-producing beta cells, PAIRs permit adaptive XBP1 mRNA splicing, while quelling destructive/terminal outputs from extra-XBP1 mRNA endonucleolytic decay, thus preventing apoptosis. Preservation of XBP1 splicing by PAIRs permits B lymphocytes to differentiate into immunoglobulin-producing plasma cells. In summary, we propose that an intermediate RNase-inhibitory “sweet spot,” achieved by PAIR-bound IRE1a, may capture a structural conformation naturally available to IRE1a that could represent a desirable therapeutic state for drugging this master UPR sensor/effector.

2021-06-01 | GSE164496 | GEO

Identification of ENO2-targeted downstream genes by ChIP-seq in Arabidopsis

Project description:ENO2, a bifunctional protein with enolase activity and transcriptional activity, plays a vital role in plant development and responses to environmental stresses. However, only several downstream genes targeted by ENO2 have been reported so far. Our study here identified hundreds of candidates of ENO2 targets with ChIP-seq and our special anti-ENO2 antibody. These results will help us further study the role of ENO2 in plant growth/development and environmental stress responses.

2022-06-04 | GSE151305 | GEO

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