ArticleThe Plant cell2013
BINDING PROTEIN is a master regulator of the endoplasmic reticulum stress sensor/transducer bZIP28 in Arabidopsis.
Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers, 1 of them a synthesis that pooled it.
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Who cites it
94 citing papers in PubMed, 1 synthesis or guideline pooled it, 167 citations in OpenAlex.
- Cell Death Signaling From Endoplasmic Reticulum Stress: Plant-Specific and Conserved Features.Frontiers in plant science · 2022Pooled it
- Unfolding Plant Defence: Endoplasmic Reticulum Stress Signalling at the Plant-Pathogen Interface.Plant biotechnology journal · 2026Review
- Redox-mediated regulation of ABSCISIC ACID-INSENSITIVE 5 affects seed germination and seedling development in Arabidopsis.Journal of experimental botany · 2026Article
- Functional Characterization ofInternational journal of molecular sciences · 2026Article
- Modulating Purothionin Accumulation and Signal Peptide Cleavage Fine-Tunes Wheat Flour Gluten Properties to Improve Cookie-Making Quality.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Article
- A Holistic Investigation of Arabidopsis Proteomes Altered in Chloroplast Biogenesis and Retrograde Signalling Identifies PsbO as a Key Regulator of Chloroplast Quality Control.Plant, cell & environment · 2025Article
- Protein homeostasis under heat stress: The role of BiP3, HsfA2, and chromatin remodeling in plants.Plant physiology · 2025Article
- The core morning clock component CCA1 enhances UPR target gene expression to facilitate ER stress recovery.Plant communications · 2025Article
- Geminivirus βV1 protein activates bZIP17/28-mediated UPR signaling to facilitate viral pathogenicity but its activity is attenuated by autophagic degradation in plants.Plant communications · 2025Article
- Molecular aspects of heat stress sensing in land plants.The Plant journal : for cell and molecular biology · 2025Review
- Subcellular Localization of Geminivirus Proteins by Laser Scanning Confocal Microscopy.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Comparative proteomics in tall fescue to reveal underlying mechanisms for improving Photosystem II thermotolerance during heat stress memory.BMC genomics · 2024Article
- Should I stay or should I go? Trafficking of plant extra-nuclear transcription factors.The Plant cell · 2024Review
- In-Depth Characterization ofPlants (Basel, Switzerland) · 2024Article
- Transcriptomics and starch biosynthesis analysis in leaves and developing seeds of mung bean provide a basis for genetic engineering of starch composition and seed quality.Frontiers in plant science · 2024Article
- Mechanisms of Endoplasmic Reticulum Protein Homeostasis in Plants.International journal of molecular sciences · 2023Review
- Transcriptional Regulators of Plant Adaptation to Heat Stress.International journal of molecular sciences · 2023Review
- Role of bZIP Transcription Factors in Plant Salt Stress.International journal of molecular sciences · 2023Review
- Synergism: biocontrol agents and biostimulants in reducing abiotic and biotic stresses in crop.World journal of microbiology & biotechnology · 2023Review
34 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BINDING PROTEIN (BiP) is a major chaperone in the endoplasmic reticulum (ER) lumen, and this study shows that BiP binds to the C-terminal tail of the stress sensor/transducer bZIP28, a membrane-associated transcription factor, retaining it in the ER under unstressed conditions. In response to ER stress, BiP dissociates from bZIP28, allowing it to be mobilized from the ER to the Golgi where it is proteolytically processed and released to enter the nucleus. Under unstressed conditions, BiP binds to bZIP28 as it binds to other client proteins, through its substrate binding domain. BiP dissociates from bZIP28 even when bZIP28's exit from the ER or its release from the Golgi is blocked. Both BiP1 and BiP3 bind bZIP28, and overexpression of either BiP detains bZIP28 in the ER under stress conditions. A C-terminally truncated mutant of bZIP28 eliminating most of the lumenal domain does not bind BiP and is not retained in the ER under unstressed conditions. BiP binding sites in the C-terminal tail of bZIP28 were identified in a phage display system. BiP was found to bind to intrinsically disordered regions on bZIP28's lumen-facing tail. Thus, the dissociation of BiP from the C-terminal tail of bZIP28 is a major switch that activates one arm of the unfolded protein response signaling pathway in plants.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.