PXD004257 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Thermal shock induces host proteostasis disruption and endoplasmic reticulum stress in the model symbiotic cnidarian Aiptasia |
Description | Coral bleaching has devastating effects on coral survival and reef ecosystem function, but many of the fundamental cellular effects of thermal stress on cnidarian physiology are unclear. We used label-free liquid chromatography-tandem mass spectrometry to assess the effects of high temperatures on the proteome of the model symbiotic anemone Aiptasia sp. Anemones were acclimated to elevated temperatures (30 °C and 33.5 °C) for two weeks or exposed to short-term thermal shock (33.5 °C, 24 hours) without acclimation. We identified 2,137 protein clusters in Aiptasia, 136 of which were differentially abundant between treatments. There were minimal differences (nine proteins) in protein abundances between the control (25 °C) and acclimated high-temperature (30 °C and 33.5 °C) treatments, indicating that thermal acclimation in symbiotic cnidarians is not primarily regulated at the level of protein expression. Heat shock resulted in significant changes in the abundance of 104 proteins, including those involved in protein folding and synthesis, redox homeostasis, and central metabolism. Nineteen highly abundant cytoskeletal and structural proteins showed particularly reduced abundance (approximately 50%), demonstrating proteostasis disruption and inhibition of protein synthesis. Heat shock induced proteins involved in multiple mechanisms for stabilizing nascent proteins, preventing protein aggregation and degrading damaged proteins, indicative of endoplasmic reticulum stress. Antioxidant mechanisms and metabolic enzymes necessary for redox homeostasis were also upregulated. Disruption of host proteostasis occurred before either bleaching or symbiont photoinhibition was detected, strongly suggesting endogenous reactive oxygen species production as the proximate cause of thermal damage. The effects of thermal shock were most pronounced at the endoplasmic reticulum, and proteostasis maintenance and protein turnover mechanisms may be essential in the response to severe thermal stress in symbiotic cnidarians. |
HostingRepository | PRIDE |
AnnounceDate | 2018-03-14 |
AnnouncementXML | Submission_2018-03-14_01:41:19.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Clinton Oakley |
SpeciesList | scientific name: Aiptasia; NCBI TaxID: 12922; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | LTQ Orbitrap |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2016-05-31 03:31:54 | ID requested | |
⏵ 1 | 2018-03-14 01:41:20 | announced | |
Publication List
Oakley CA, Durand E, Wilkinson SP, Peng L, Weis VM, Grossman AR, Davy SK, Thermal Shock Induces Host Proteostasis Disruption and Endoplasmic Reticulum Stress in the Model Symbiotic Cnidarian Aiptasia. J Proteome Res, 16(6):2121-2134(2017) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: Cnidarian-dinoflagellate symbiosis, coral reefs, model organisms, thermal stress |
Contact List
Simon Keith Davy |
contact affiliation | School of Biological Sciences Victoria University of Wellington |
contact email | simon.davy@vuw.ac.nz |
lab head | |
Clinton Oakley |
contact affiliation | Victoria University of Wellington |
contact email | clint.oakley@gmail.com |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD004257
- Label: PRIDE project
- Name: Thermal shock induces host proteostasis disruption and endoplasmic reticulum stress in the model symbiotic cnidarian Aiptasia