Thermal stress induces tissue damage and a broad shift in regenerative signaling pathways in the honey bee intestine
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA667676 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR12780027.fastq.gz | Fastqsanger.gz | |||
| SRR12780028.fastq.gz | Fastqsanger.gz | |||
| SRR12780029.fastq.gz | Fastqsanger.gz | |||
| SRR12780030.fastq.gz | Fastqsanger.gz | |||
| SRR12780031.fastq.gz | Fastqsanger.gz |
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Project description:Honey bee colonies in the United States have suffered from a higher than usual rate of die-off in the last few years with a complex set of interacting stresses playing a key role. With changing climate, an increase in the frequency of severe weather events, such as heat waves, is anticipated and understanding how these changes may contribute to stress in the bee is of crucial. Individual honey bees appear to have a high capacity to endure thermal stress. One reason for this high-level endurance is likely their robust HSR which contributes to thermotolerance at the cellular level. To elucidate other determinants of this resilience, we used thermal stress coupled with RNAseq and identified broad transcriptional remodeling of a number of key signaling pathways in the honey bee in response to tissue damage, including those pathways known to be involved in digestive tract regeneration in the fruit fly such as the Hippo and JAK-STAT pathways. We also observe cell death and shedding of epithelial cells, which likely leads to induction of this regenerative program. We found that thermal stress affects many of these pathways in other tissues, suggesting a shared program of damage response. In addition to allowing for important foundational characterization of damage response program in this key pollinating species, this study suggest that a robust regeneration program may also be a critical contributor to thermotolerance at the tissue level.
2021-09-08 | GSE159083 | GEO
Project description:In this study, we sought to identify how protein thermal stability integrates with changes in cell signaling and protein abundance. We developed a pipeline to investigate changes in protein abundance and thermal stabilite by combining the protein abundance and thermal shift measurements into the same TMT-plex in the Integrated Thermal Shift Assay (ITSA). Additionally, to elucidate how protein signaling corresponds to changes in thermal stability we also examined protein phosphorylation in the Phosphorylation Integrated Thermal Shift Assay (PITSA).
2024-06-17 | PXD050772 | Pride
Project description:Existing thermal shift-based mass spectrometry approaches are able to identify target proteins without chemical modification of the ligand, but they are suffering from complicated workflows with limited throughput. Herein, we present a new thermal shift-based method, termed matrix thermal shift assay (mTSA), for fast deconvolution of ligand-binding targets and binding affinities at the proteome level. In mTSA, a sample matrix, treated horizontally with five different compound concentrations and vertically with five technical replicates of each condition, was denatured at a single temperature to induce protein precipitation, and then, data-independent acquisition was employed for quick protein quantification. Compared with previous thermal shift assays, the analysis throughput of mTSA was significantly improved, but the costs as well as efforts were reduced. More importantly, the matrix experiment design allowed simultaneous computation of the statistical significance and fitting of the dose–response profiles, which can be combined to enable a more accurate identification of target proteins, as well as reporting binding affinities between the ligand and individual targets. Using a pan-specific kinase inhibitor, staurosporine, we demonstrated a 36% improvement in screening sensitivity over the traditional thermal proteome profiling (TPP) and a comparable sensitivity with a latest two-dimensional TPP. Finally, mTSA was successfully applied to delineate the target landscape of perfluorooctanesulfonic acid (PFOS), a persistent organic pollutant that is hard to perform modification on, and revealed several potential targets that might account for the toxicities of PFOS.
2023-09-29 | PXD045941 |
Project description:This project describes a novel thermal shift assay for proteome-wide deconvolution of drug binding targets.
2021-12-21 | PXD027018 | JPOST Repository
Project description:Here, we investigate the genetic mechanisms that underlie thermal specialization of closely-related vibrios isolated from coastal water at the Beaufort Inlet (Beaufort, NC, USA). This location experiences large seasonal temperature fluctuations (annual range of ~20°C), and a clear seasonal shift in vibrio diversity has been observed (Yung et al. 2015). This previous study suggested that the mechanisms of thermal adaptation apparently differ based on evolutionary timescale: shifts in the temperature of maximal growth occur between deeply branching clades but the shape of the thermal performance curve changes on shorter time scales (Yung et al. 2015). The observed thermal specialization in vibrio populations over relatively short evolutionary time scales indicates that few genes or cellular processes may contribute to the differences in thermal performance between populations. In order to understand the molecular mechanisms that underlie adaptation to local thermal regimes in environmental vibrio populations, we employ genomic and transcriptomic approaches to examine transcriptomic changes that occur within strains grown at their thermal optima and under heat and cold stress. Moreover, we compare two closely-related strains with different laboratory thermal preferences to identify in situ evolutionary responses to different thermal environments in genome content and alleles as well as gene expression.
2018-07-31 | GSE83396 | GEO
Project description:In response to an ever-increasing demand of new small molecules therapeutics, numerous chemical and genetic tools have been developed to interrogate compound mechanism of action. Owing to its ability to characterize compound-dependent changes in thermal stability, the proteome-wide thermal shift assay has emerged as a powerful tool in this arsenal. The most recent iterations have drastically improved the overall efficiency of these assays, providing an opportunity to screen compounds at a previously unprecedented rate. Taking advantage of this advance, we quantified 1.498 million thermal stability measurements in response to multiple classes of therapeutic and tool compounds (96 compounds in living cells and 70 compounds in lysates). When interrogating the dataset as a whole, approximately 80% of compounds (with quantifiable targets) caused a significant change in the thermal stability of an annotated target. There was also a wealth of evidence portending off-target engagement despite the extensive use of the compounds in the laboratory and/or clinic. Finally, the combined application of cell- and lysate-based assays, aided in the classification of primary (direct ligand binding) and secondary (indirect) changes in thermal stability. Overall, this study highlights the value of these assays in the drug development process by affording an unbiased and reliable assessment of compound mechanism of action.
2025-02-13 | PXD048009 | Pride
Project description:Urbanization is one of the most significant land cover transformations, and while climate alteration is one of its most cited ecological consequences we have very limited knowledge on its effect on species' thermal responses. We investigated whether changes in environmental thermal variability caused by urbanization influence thermal tolerance in honey bees (Apis mellifera) in a semi-arid city in central Mexico. Ambient environmental temperature and honey bee thermal tolerance were compared in urban and rural sites. Ambient temperature variability decreased with urbanization due to significantly higher nighttime temperatures in urban compared to rural sites and not from differences in maximum daily temperatures. Honey bee thermal tolerance breadth [critical thermal maxima (CTmax)-critical thermal minima (CTmin)] was narrower for urban bees as a result of differences in cold tolerance, with urban individuals having significantly higher CTmin than rural individuals, and CTmax not differing among urban and rural individuals. Honey bee body size was not correlated to thermal tolerance, and body size did not differ between urban and rural individuals. We found that honey bees' cold tolerance is modified through acclimation. Our results show that differences in thermal variability along small spatial scales such as urban-rural gradients can influence species' thermal tolerance breadths.
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Project description:Samples are from a screening experiment on 5 laboratory cultures of the coral endosymbiont: Symbiodiniaceae (Symbiodinium linuchae, Breviolum psygmophilum, Durusdinium trenchii, Effrenium voratum and Fugacium kawagutii). Samples are also from a thermal stress experiment (increased temperatures from 26 to 32 degrees C) carried out on Durusdinium trenchii and Cladocopium goreaui, two common coral endosymbionts on the Great Barrier Reef. All samples were collected on Markes Tenax TA thermal desorption tubes.
Lawson, C.A., Possell, M., Seymour, J.R., Raina, J.B. and Suggett, D.J., 2019. Coral endosymbionts (Symbiodiniaceae) emit species-specific volatilomes that shift when exposed to thermal stress. Scientific reports, 9(1), pp.1-11.
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Project description:Despite the growing interest in using chemical genetics in plant research, small-molecule target identification remains a major challenge. The cellular thermal shift assay coupled with high-resolution massspectrometry (CETSA MS) that monitors changes in the thermal stability of proteins caused by their interactions with small molecules, other proteins, or post-translational modifications allows the identification of drug targets, or the study of protein-metabolite and protein-protein interactions mainly in mammalian cells. To showcase the applicability of this method in plants, we applied CETSA MS to intact Arabidopsis thaliana cells and identified the thermal proteome of the plant-specific glycogen synthase kinase 3 (GSK3) inhibitor, bikinin. A comparison between the thermal- and the phospho-proteomes of bikinin revealed the auxin efflux carrier PIN-FORMED1 (PIN1) as a novel substrate of the Arabidopsis GSK3s that negatively regulate the brassinosteroid signaling. We established that PIN1 phosphorylation by the GSK3s is essential for maintaining its intracellular polarity that is required for auxin-mediated regulation of vascular patterning in the leaf thus, revealing a novel crosstalk between brassinosteroid and auxin signaling.
2022-04-04 | PXD030309 | Pride