<?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: Stress sensor Ire1 deploys a divergent transcriptional program in response to lipid bilayer stress</titl><IDNo agency="DOI">doi:10.21979/N9/5BJD2Z</IDNo></titlStmt><distStmt><distrbtr source="archive">DR-NTU (Data)</distrbtr><distDate>2020-06-18</distDate></distStmt><verStmt source="archive"><version date="2020-06-18" type="RELEASED">1</version></verStmt><biblCit>Ho, Nurulain; Yap, Wei Sheng; Xu, Jiaming; Wu, Haoxi; Koh, Jhee Hong; George, Bhawana; Chong, Shu Chen; Taubert, Stefan; Thibault, Guillaume, 2020, "Replication Data for: Stress sensor Ire1 deploys a divergent transcriptional program in response to lipid bilayer stress", https://doi.org/10.21979/N9/5BJD2Z, DR-NTU (Data), V1</biblCit></citation></docDscr><stdyDscr><citation><titlStmt><titl>Replication Data for: Stress sensor Ire1 deploys a divergent transcriptional program in response to lipid bilayer stress</titl><altTitl>Distinct UPR program activated by LBS</altTitl><IDNo agency="DOI">doi:10.21979/N9/5BJD2Z</IDNo></titlStmt><rspStmt><AuthEnty affiliation="Nanyang Technological University">Ho, Nurulain</AuthEnty><AuthEnty affiliation="Nanyang Technological University">Yap, Wei Sheng</AuthEnty><AuthEnty affiliation="University of British Columbia">Xu, Jiaming</AuthEnty><AuthEnty affiliation="Nanyang Technological University">Wu, Haoxi</AuthEnty><AuthEnty affiliation="Nanyang Technological University">Koh, Jhee Hong</AuthEnty><AuthEnty affiliation="Nanyang Technological University">George, Bhawana</AuthEnty><AuthEnty affiliation="Nanyang Technological University">Chong, Shu Chen</AuthEnty><AuthEnty affiliation="University of British Columbia">Taubert, Stefan</AuthEnty><AuthEnty affiliation="Nanyang Technological University">Thibault, Guillaume</AuthEnty></rspStmt><prodStmt><software version="2013">Microsoft excel</software><software version="6">Graphpad Prism</software><grantNo agency="Nanyang Technological University">Nanyang Assistant Professorship program</grantNo><grantNo agency="National Research Foundation (NRF)">NRF2018NRFNSFC003SB-006</grantNo><grantNo agency="National Natural Science Foundation of China">NRF-NSFC</grantNo><grantNo agency="Nanyang Technological University">Research Scholarship (predoctoral fellowship)</grantNo><grantNo agency="Canadian Institutes of Health Research">PJT-153199</grantNo><grantNo agency="National Institutes of Health Office of Research Infrastructure Programs">P40 OD010440</grantNo></prodStmt><distStmt><distrbtr source="archive">DR-NTU (Data)</distrbtr><contact affiliation="Nanyang Technological University">Guillaume Thibault</contact><depositr>Yap, Wei Sheng</depositr><depDate>2020-06-01</depDate></distStmt><holdings URI="https://doi.org/10.21979/N9/5BJD2Z"/></citation><stdyInfo><subject><keyword xml:lang="en">Medicine, Health and Life Sciences</keyword><keyword>Medicine, Health and Life Sciences</keyword><keyword>Unfolded protein response; lipid bilayer stress; endoplasmic reticulum stress; endoplasmic reticulum sensor Ire1; UPR-transducer; proteotoxic stress; membrane stress; phospholipid perturbation; S. cerevisiae; C. elegans</keyword></subject><abstract date="2020-06-18">Membrane integrity at the endoplasmic reticulum (ER) is tightly regulated, and its disturbance is implicated in metabolic diseases. Using an engineered sensor that activates the unfolded protein response (UPR) exclusively when normal ER membrane lipid composition is compromised, we identified pathways beyond lipid metabolism that are necessary to maintain ER integrity in yeast and in C. elegans. To systematically validate yeast mutants that disrupt ER membrane homeostasis, we identified a lipid bilayer stress (LBS) sensor in the UPR transducer protein Ire1, located at the interface of the amphipathic and transmembrane helices. Furthermore, transcriptome and chromatin immunoprecipitation analyses pinpoint the UPR as a broad-spectrum compensatory response wherein LBS and proteotoxic stress deploy divergent transcriptional UPR programs. Together, these findings reveal the UPR program as the sum of two independent stress responses, an insight that could be exploited for future therapeutic intervention.</abstract><sumDscr><dataKind>Excel</dataKind><dataKind>Prism</dataKind></sumDscr></stdyInfo><method><dataColl><sources/></dataColl><anlyInfo/></method><dataAccs><setAvail/><useStmt/></dataAccs><othrStdyMat><relPubl><citation><titlStmt><IDNo agency="doi">10.1083/jcb.201909165</IDNo></titlStmt><biblCit>Ho, N., Yap, W. S., Xu, J., Wu, H., Koh, J. H., Goh, W. W. B., ... & Thibault, G. (2020). Stress sensor Ire1 deploys a divergent transcriptional program in response to lipid bilayer stress. Journal of Cell Biology, 219(7).</biblCit></citation><ExtLink URI="https://rupress.org/jcb/article/219/7/e201909165/151719/Stress-sensor-Ire1-deploys-a-divergent"/></relPubl><relPubl><citation><titlStmt><IDNo agency="handle">10356/149106</IDNo></titlStmt><biblCit>Ho, N., Yap, W. S., Xu, J., Wu, H., Koh, J. H., Goh, W. W. B., ... & Thibault, G. (2020). Stress sensor Ire1 deploys a divergent transcriptional program in response to lipid bilayer stress. Journal of Cell Biology, 219(7).</biblCit></citation><ExtLink URI="https://hdl.handle.net/10356/149106"/></relPubl></othrStdyMat></stdyDscr><otherMat ID="f37649" URI="https://researchdata.ntu.edu.sg/api/access/datafile/37649" level="datafile"><labl>Figure 1.zip</labl><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f37650" URI="https://researchdata.ntu.edu.sg/api/access/datafile/37650" level="datafile"><labl>Figure 2.zip</labl><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f37651" URI="https://researchdata.ntu.edu.sg/api/access/datafile/37651" level="datafile"><labl>Figure 3.zip</labl><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f37646" URI="https://researchdata.ntu.edu.sg/api/access/datafile/37646" level="datafile"><labl>Figure 4.zip</labl><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f37647" URI="https://researchdata.ntu.edu.sg/api/access/datafile/37647" level="datafile"><labl>Figure 5.zip</labl><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f37648" URI="https://researchdata.ntu.edu.sg/api/access/datafile/37648" level="datafile"><labl>Figure 6.zip</labl><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f37644" URI="https://researchdata.ntu.edu.sg/api/access/datafile/37644" level="datafile"><labl>Figure S1.zip</labl><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f37645" URI="https://researchdata.ntu.edu.sg/api/access/datafile/37645" level="datafile"><labl>Figure S2.zip</labl><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f37641" URI="https://researchdata.ntu.edu.sg/api/access/datafile/37641" level="datafile"><labl>Figure S3.zip</labl><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f37642" URI="https://researchdata.ntu.edu.sg/api/access/datafile/37642" level="datafile"><labl>Figure S4.zip</labl><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat><otherMat ID="f37643" URI="https://researchdata.ntu.edu.sg/api/access/datafile/37643" level="datafile"><labl>Figure S5.zip</labl><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/zip</notes></otherMat></codeBook>