<?xml version='1.0' encoding='UTF-8'?><codeBook xmlns="ddi:codebook:2_5" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="ddi:codebook:2_5 https://ddialliance.org/Specification/DDI-Codebook/2.5/XMLSchema/codebook.xsd" version="2.5"><docDscr><citation><titlStmt><titl>Replication Data for: The yeast FIT2 homologs are necessary to maintain cellular proteostasis and membrane lipid homeostasis</titl><IDNo agency="DOI">doi:10.21979/N9/I7MXVP</IDNo></titlStmt><distStmt><distrbtr source="archive">DR-NTU (Data)</distrbtr><distDate>2020-10-19</distDate></distStmt><verStmt source="archive"><version date="2020-11-13" type="RELEASED">2</version></verStmt><biblCit>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</biblCit></citation></docDscr><stdyDscr><citation><titlStmt><titl>Replication Data for: The yeast FIT2 homologs are necessary to maintain cellular proteostasis and membrane lipid homeostasis</titl><IDNo agency="DOI">doi:10.21979/N9/I7MXVP</IDNo></titlStmt><rspStmt><AuthEnty affiliation="Nanyang Technological University">Thibault, Guillaume</AuthEnty><AuthEnty affiliation="Nanyang Technological University">Yap, Wei Sheng</AuthEnty><AuthEnty affiliation="Nanyang Technological University">Shuy, Peter Jr.</AuthEnty><AuthEnty affiliation="Nanyang Technological University">Marvalim, Charlie</AuthEnty></rspStmt><prodStmt><software>GraphPad</software><grantNo agency="Nanyang Technological University">Nanyang Assistant Professorship programme</grantNo><grantNo agency="National Research Foundation (NRF)">NRF-NSFC joint research grant NRF2018NRFNSFC003SB-006</grantNo><grantNo agency="Nanyang Technological University">Research Scholarship (predoctoral fellowship)</grantNo><grantNo agency="National Institutes of Health (NIH)">GM-19629</grantNo></prodStmt><distStmt><distrbtr source="archive">DR-NTU (Data)</distrbtr><contact affiliation="Nanyang Technological University">Thibault, Guillaume</contact><depositr>Thibault, Guillaume</depositr><depDate>2020-09-12</depDate></distStmt><holdings URI="https://doi.org/10.21979/N9/I7MXVP"/></citation><stdyInfo><subject><keyword xml:lang="en">Medicine, Health and Life Sciences</keyword><keyword>Medicine, Health and Life Sciences</keyword><keyword>endoplasmic reticulum-associated degradation (ERAD)</keyword><keyword>lipid droplet</keyword><keyword>proteostasis</keyword><keyword>phospholipid metabolism</keyword><keyword>Scs3</keyword><keyword>unfolded protein response (UPR)</keyword></subject><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.</abstract><sumDscr><dataKind>experimental data</dataKind></sumDscr></stdyInfo><method><dataColl><sources/></dataColl><anlyInfo/></method><dataAccs><setAvail/><useStmt/></dataAccs><othrStdyMat><relPubl><citation><titlStmt><IDNo agency="doi">10.1242/jcs.248526</IDNo></titlStmt><biblCit>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).</biblCit></citation><ExtLink URI="https://jcs.biologists.org/content/133/21/jcs248526.abstract"/></relPubl><relPubl><citation><titlStmt><IDNo agency="handle">10356/161980</IDNo></titlStmt><biblCit>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-.</biblCit></citation><ExtLink URI="https://hdl.handle.net/10356/161980"/></relPubl></othrStdyMat></stdyDscr><otherMat ID="f54834" URI="https://researchdata.ntu.edu.sg/api/access/datafile/54834" level="datafile"><labl>Figure 1.zip</labl><txt>Data for 'Fig. 1. Scs3 is essential for viability in the absence of UPR transducer Ire1.'</txt><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f54837" URI="https://researchdata.ntu.edu.sg/api/access/datafile/54837" level="datafile"><labl>Figure 2A.zip</labl><txt>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.</txt><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f54833" URI="https://researchdata.ntu.edu.sg/api/access/datafile/54833" level="datafile"><labl>Figure 3 and S5 (MYTH).zip</labl><txt>Data for 'Fig. 3. The ScFIT interactome as identified by membrane yeast two-hybrid screening.' and 'Fig. S5. Validation of ScFIT protein interactor specificity.'</txt><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f54830" URI="https://researchdata.ntu.edu.sg/api/access/datafile/54830" level="datafile"><labl>Figure 4.zip</labl><txt>Data for 'Fig. 4. The clearance of ERAD client proteins is impaired in ScFIT mutants.'</txt><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f54836" URI="https://researchdata.ntu.edu.sg/api/access/datafile/54836" level="datafile"><labl>Figure 5.zip</labl><txt>Data for 'Fig. 5. Scs3 is sufficient to rescue proteostatic defect ofScFITΔ.'</txt><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f54832" URI="https://researchdata.ntu.edu.sg/api/access/datafile/54832" level="datafile"><labl>FIgure S1.zip</labl><txt>Data for 'Fig. S1. HSR activation is dampened in ScFITΔ mutants'</txt><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f54835" URI="https://researchdata.ntu.edu.sg/api/access/datafile/54835" level="datafile"><labl>Figure S2.zip</labl><txt>Data for 'Fig. S2. Colony sectoring assay reveals essentiality of IRE1 in the absence of SCS3.'</txt><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f54831" URI="https://researchdata.ntu.edu.sg/api/access/datafile/54831" level="datafile"><labl>Figure S3.zip</labl><txt>Data for 'Fig. S3. Separation of triacylglycerol by thin layer chromatography.'</txt><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f54838" URI="https://researchdata.ntu.edu.sg/api/access/datafile/54838" level="datafile"><labl>Figure S6.zip</labl><txt>Data for 'Fig. S6. ScFITΔ mutants can degrade natively folded proteins.'</txt><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat></codeBook>