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Part 1: Document Description
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Citation |
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Title: |
Replication Data for: The yeast FIT2 homologs are necessary to maintain cellular proteostasis and membrane lipid homeostasis |
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Identification Number: |
doi:10.21979/N9/I7MXVP |
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Distributor: |
DR-NTU (Data) |
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Date of Distribution: |
2020-10-19 |
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Version: |
2 |
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Bibliographic Citation: |
Thibault, Guillaume; Yap, Wei Sheng; Shuy, Peter Jr.; Marvalim, Charlie, 2020, "Replication Data for: The yeast FIT2 homologs are necessary to maintain cellular proteostasis and membrane lipid homeostasis", https://doi.org/10.21979/N9/I7MXVP, DR-NTU (Data), V2 |
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Citation |
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Title: |
Replication Data for: The yeast FIT2 homologs are necessary to maintain cellular proteostasis and membrane lipid homeostasis |
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Identification Number: |
doi:10.21979/N9/I7MXVP |
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Authoring Entity: |
Thibault, Guillaume (Nanyang Technological University) |
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Yap, Wei Sheng (Nanyang Technological University) |
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Shuy, Peter Jr. (Nanyang Technological University) |
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Marvalim, Charlie (Nanyang Technological University) |
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Software used in Production: |
GraphPad |
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Grant Number: |
Nanyang Assistant Professorship programme |
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Grant Number: |
NRF-NSFC joint research grant NRF2018NRFNSFC003SB-006 |
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Grant Number: |
Research Scholarship (predoctoral fellowship) |
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Grant Number: |
GM-19629 |
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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: |
2020-09-12 |
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Holdings Information: |
https://doi.org/10.21979/N9/I7MXVP |
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Study Scope |
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Keywords: |
Medicine, Health and Life Sciences, Medicine, Health and Life Sciences, endoplasmic reticulum-associated degradation (ERAD), lipid droplet, proteostasis, phospholipid metabolism, Scs3, unfolded protein response (UPR) |
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Abstract: |
Lipid droplets (LDs) are implicated in conditions of lipid and protein dysregulation. The fat storage inducing transmembrane (FIT) family induces LD formation. Here, we establish a model system to study the role of S. cerevisiae FIT homologues (ScFIT), SCS3 and YFT2, in proteostasis and stress response pathways. While LD biogenesis and basal endoplasmic reticulum (ER) stress-induced unfolded protein response (UPR) remain unaltered in ScFIT mutants, SCS3 was found essential for proper stress-induced UPR activation and for viability in the absence of the sole yeast UPR transducer IRE1. Devoid of a functional UPR, muted SCS3 exhibited accumulation of triacylglycerol within the ER along with aberrant LD morphology, suggesting a UPR-dependent compensatory mechanism. Additionally, SCS3 was necessary to maintain phospholipid homeostasis. Strikingly, global protein ubiquitination and the turnover of both ER and cytoplasmic misfolded proteins is impaired in ScFITΔ cells, while a screen for interacting partners of Scs3 identifies components of the proteostatic machinery as putative targets. Together, our data support a model where ScFITs play an important role in lipid metabolism and proteostasis beyond their defined roles in LD biogenesis. |
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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: |
10.1242/jcs.248526 |
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Bibliographic Citation: |
Yap, W. S., Shyu, P., Gaspar, M. L., Jesch, S. A., Marvalim, C., Prinz, W. A., ... & Thibault, G. (2020). The yeast FIT2 homologs are necessary to maintain cellular proteostasis and membrane lipid homeostasis. Journal of Cell Science, 133(21). |
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Citation |
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Identification Number: |
10356/161980 |
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Bibliographic Citation: |
Yap, W. S., Shyu Jr., P., Gaspar, M. L., Jesch, S. A., Marvalim, C., Prinz, W. A., Henry, S. A. & Thibault, G. (2020). The yeast FIT2 homologs are necessary to maintain cellular proteostasis and membrane lipid homeostasis. Journal of Cell Science, 133(21), jcs248526-. |
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Label: |
Figure 1.zip |
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Text: |
Data for 'Fig. 1. Scs3 is essential for viability in the absence of UPR transducer Ire1.' |
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Notes: |
application/zip |
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Figure 2A.zip |
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Text: |
Data for 'Fig. 2. Scs3 is necessary to maintain lipid homeostasis and LD morphology.' Exclude TEM data due to huge file size, available upon request. |
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Notes: |
application/zip |
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Figure 3 and S5 (MYTH).zip |
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Data for 'Fig. 3. The ScFIT interactome as identified by membrane yeast two-hybrid screening.' and 'Fig. S5. Validation of ScFIT protein interactor specificity.' |
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Notes: |
application/zip |
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Figure 4.zip |
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Text: |
Data for 'Fig. 4. The clearance of ERAD client proteins is impaired in ScFIT mutants.' |
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Notes: |
application/zip |
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Figure 5.zip |
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Text: |
Data for 'Fig. 5. Scs3 is sufficient to rescue proteostatic defect ofScFITΔ.' |
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Notes: |
application/zip |
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FIgure S1.zip |
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Data for 'Fig. S1. HSR activation is dampened in ScFITΔ mutants' |
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Notes: |
application/zip |
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Figure S2.zip |
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Data for 'Fig. S2. Colony sectoring assay reveals essentiality of IRE1 in the absence of SCS3.' |
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Notes: |
application/zip |
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Figure S3.zip |
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Data for 'Fig. S3. Separation of triacylglycerol by thin layer chromatography.' |
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Notes: |
application/zip |
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Label: |
Figure S6.zip |
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Text: |
Data for 'Fig. S6. ScFITΔ mutants can degrade natively folded proteins.' |
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Notes: |
application/zip |