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Part 1: Document Description
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Citation |
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Title: |
Membrane phospholipid alteration causes chronic ER stress through early degradation of homeostatic ER-resident proteins |
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Identification Number: |
doi:10.21979/N9/OSZXZT |
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Distributor: |
DR-NTU (Data) |
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Date of Distribution: |
2021-04-20 |
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Version: |
1 |
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Bibliographic Citation: |
Thibault, Guillaume, 2021, "Membrane phospholipid alteration causes chronic ER stress through early degradation of homeostatic ER-resident proteins", https://doi.org/10.21979/N9/OSZXZT, DR-NTU (Data), V1 |
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Citation |
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Title: |
Membrane phospholipid alteration causes chronic ER stress through early degradation of homeostatic ER-resident proteins |
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Identification Number: |
doi:10.21979/N9/OSZXZT |
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Authoring Entity: |
Thibault, Guillaume (Nanyang Technological University) |
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Software used in Production: |
Licor, Zeiss, Excel |
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Grant Number: |
Nanyang Assistant Professorship |
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Grant Number: |
Research Scholarship |
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Grant Number: |
under its NRF-NSFC joint research grant call (Synthetic Biology) [NRF2018NRF-NSFC003SB-006] |
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Distributor: |
DR-NTU (Data) |
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Access Authority: |
Thibault, Guillaume |
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Depositor: |
Thibault, Guillaume |
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Date of Deposit: |
2021-04-20 |
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Holdings Information: |
https://doi.org/10.21979/N9/OSZXZT |
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Study Scope |
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Keywords: |
Medicine, Health and Life Sciences, Medicine, Health and Life Sciences, Transmembrane protein degradation, Sbh1, phosphatidylcholine imbalance, chronic ER 28 stress, unfolded protein response, ER protein quality control, ERAD, Doa10 complex, NAFLD, NASH |
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Abstract: |
Phospholipid homeostasis in biological membranes is essential to maintain functions of organelles such as the endoplasmic reticulum. Phospholipid perturbation has been associated to cellular stress responses. However, in most cases, the implication of membrane lipid changes to homeostatic cellular response has not been clearly defined. Previously, we reported that Saccharomyces cerevisiae adapts to lipid bilayer stress by upregulating several protein quality control pathways such as the endoplasmic reticulum-associated degradation (ERAD) pathway and the unfolded protein response (UPR). Surprisingly, we observed certain ER-resident transmembrane proteins, which form part of the UPR programme, to be destabilised under lipid bilayer stress. Among these, the protein translocon subunit Sbh1 was prematurely degraded by membrane stiffening at the ER. Moreover, our findings suggest that the Doa10 complex recognises free Sbh1 that becomes increasingly accessible during lipid bilayer stress, perhaps due to the change in ER membrane properties. Premature removal of key ER-resident transmembrane proteins might be an underlying cause of chronic ER stress as a result of lipid bilayer stress. |
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Kind of Data: |
Experimental data |
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Methodology and Processing |
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Sources Statement |
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Data Access |
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Other Study Description Materials |
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Related Publications |
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Citation |
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Identification Number: |
10.1038/s41598-019-45020-6 |
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Bibliographic Citation: |
Shyu Jr., P., Ng, B. S. H., Ho, N., Chaw, R., Seah, Y. L., Marvalim, C., & Thibault, G. (2019). Membrane phospholipid alteration causes chronic ER stress through early degradation of homeostatic ER-resident proteins. Scientific Reports, 9(1), 8637-. |
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Citation |
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Identification Number: |
10356/89646 |
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Bibliographic Citation: |
Shyu Jr., P., Ng, B. S. H., Ho, N., Chaw, R., Seah, Y. L., Marvalim, C., & Thibault, G. (2019). Membrane phospholipid alteration causes chronic ER stress through early degradation of homeostatic ER-resident proteins. Scientific Reports, 9(1), 8637-. |
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Label: |
SR Data |
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Notes: |
application/x-7z-compressed |