Related Experiment Video
Updated: Jun 13, 2025

10:36
Measurements of Physiological Stress Responses in C. Elegans
Published on: May 21, 2020
13.9K
Integrated Dual-Channel Retrograde Signaling Directs Stress Responses by Degrading the HAT1/TPL/IMPα-9 Suppressor
Biorxiv : the Preprint Server for Biology
|September 11, 2024
Summary
The metabolite MEcPP (MECPP) triggers plant stress responses by dismantling a suppressor complex, releasing an activator, and enhancing calcium signaling for gene expression. This process is vital for maintaining cellular balance during stress.
Area of Science:
- Plant molecular biology
- Cellular signaling
- Stress response mechanisms
Background:
- Plastid-nucleus communication is crucial for regulating gene expression during stress.
- The Rapid Stress Response Element (RSRE) is a key regulatory hub in stress signaling.
- The role of specific metabolites in coordinating these pathways remains incompletely understood.
Purpose of the Study:
- To elucidate the mechanism by which the plastidial metabolite MEcPP activates the RSRE.
- To identify the components of the suppressor complex that regulates RSRE activity.
- To understand how MEcPP integrates plastidial signals with nuclear responses.
Main Methods:
- Genetic analysis
- Biochemical assays
- Cellular biology techniques
- Protein modeling
Main Results:
- Identified the HAT1/TPL/IMPα-9 complex as a repressor of RSRE and its activator CAMTA3.
- Demonstrated that stress-induced MEcPP disrupts this suppressor complex.
- Showed that MEcPP enhances Ca 2+ influx, leading to CAMTA3 activation and RSRE-mediated gene transcription.
Conclusions:
- MEcPP acts as a signaling molecule, coordinating plastid-to-nucleus communication under stress.
- The disruption of the HAT1/TPL/IMPα-9 complex by MEcPP is a critical step in activating stress-responsive genes.
- This pathway highlights a dual role for MEcPP in both biochemical function and signal initiation for cellular homeostasis.
Related Concept Videos
Interactions Between Signaling Pathways
6.2K
Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
6.2K
MAPK Signaling Cascades
5.3K
Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
5.3K
Calmodulin-dependent Signaling
5.1K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.1K
Regulation of the Unfolded Protein Response
2.4K
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.4K
TGF - β Signaling Pathway
7.3K
The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
7.3K
The Unfolded Protein Response
4.5K
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
4.5K

