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Titel: A Quantitative Analysis of Cellular Lipid Compositions During Acute Proteotoxic ER Stress Reveals Specificity in the Production of Asymmetric Lipids
VerfasserIn: Reinhard, John
Mattes, Carsten
Väth, Kristina
Radanović, Toni
Surma, Michal A.
Klose, Christian
Ernst, Robert
Sprache: Englisch
Titel: Frontiers in Cell and Developmental Biology
Bandnummer: 8
Verlag/Plattform: Frontiers
Erscheinungsjahr: 2020
Freie Schlagwörter: UPR
Ire1
lipid bilayer stress
proteotoxic stress
lipidomics
DTT
tunicamycin
asymmetric lipids
DDC-Sachgruppe: 610 Medizin, Gesundheit
Dokumenttyp: Journalartikel / Zeitschriftenartikel
Abstract: The unfolded protein response (UPR) is central to endoplasmic reticulum (ER) homeostasis by controlling its size and protein folding capacity. When activated by unfolded proteins in the ER-lumen or aberrant lipid compositions, the UPR adjusts the expression of hundreds of target genes to counteract ER stress. The proteotoxic drugs dithiothreitol (DTT) and tunicamycin (TM) are commonly used to induce misfolding of proteins in the ER and to study the UPR. However, their potential impact on the cellular lipid composition has never been systematically addressed. Here, we report the quantitative, cellular lipid composition of Saccharomyces cerevisiae during acute, proteotoxic stress in both rich and synthetic media. We show that DTT causes rapid remodeling of the lipidome when used in rich medium at growthinhibitory concentrations, while TM has only a marginal impact on the lipidome under our conditions of cultivation. We formulate recommendations on how to study UPR activation by proteotoxic stress without interferences from a perturbed lipid metabolism. Furthermore, our data suggest an intricate connection between the cellular growth rate, the abundance of the ER, and the metabolism of fatty acids. We show that Saccharomyces cerevisiae can produce asymmetric lipids with two saturated fatty acyl chains differing substantially in length. These observations indicate that the pairing of saturated fatty acyl chains is tightly controlled and suggest an evolutionary conservation of asymmetric lipids and their biosynthetic machineries.
DOI der Erstveröffentlichung: 10.3389/fcell.2020.00756
URL der Erstveröffentlichung: https://doi.org/10.3389/fcell.2020.00756
Link zu diesem Datensatz: urn:nbn:de:bsz:291--ds-422341
hdl:20.500.11880/37919
http://dx.doi.org/10.22028/D291-42234
ISSN: 2296-634X
Datum des Eintrags: 21-Jun-2024
Bezeichnung des in Beziehung stehenden Objekts: Supplementary Material
In Beziehung stehendes Objekt: https://www.frontiersin.org/articles/file/downloadfile/559605_supplementary-materials_datasheets_1_pdf/octet-stream/Data%20Sheet%201.PDF/1/559605?isPublishedV2=False
https://www.frontiersin.org/articles/file/downloadfile/559605_supplementary-materials_datasheets_2_xlsx/octet-stream/Data%20Sheet%202.xlsx/2/559605?isPublishedV2=False
Fakultät: M - Medizinische Fakultät
Fachrichtung: M - Medizinische Biochemie und Molekularbiologie
Professur: M - Prof. Dr. Robert Ernst
Sammlung:SciDok - Der Wissenschaftsserver der Universität des Saarlandes

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