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Titel: Systematic analysis of membrane contact sites in Saccharomyces cerevisiae uncovers modulators of cellular lipid distribution
VerfasserIn: Castro, Inês Gomes
Shortill, Shawn P.
Dziurdzik, Samantha Katarzyna
Cadou, Angela
Ganesan, Suriakarthiga
Valenti, Rosario
David, Yotam
Davey, Michael
Mattes, Carsten
Thomas, Ffion B.
Avraham, Reut Ester
Meyer, Hadar
Fadel, Amir
Fenech, Emma J.
Ernst, Robert
Zaremberg, Vanina
Levine, Tim P.
Stefan, Christopher
Conibear, Elizabeth
Schuldiner, Maya
Sprache: Englisch
Titel: eLife
Bandnummer: 11
Verlag/Plattform: eLife Sciences Publications
Erscheinungsjahr: 2022
DDC-Sachgruppe: 610 Medizin, Gesundheit
Dokumenttyp: Journalartikel / Zeitschriftenartikel
Abstract: Actively maintained close appositions between organelle membranes, also known as contact sites, enable the efficient transfer of biomolecules between cellular compartments. Several such sites have been described as well as their tethering machineries. Despite these advances we are still far from a comprehensive understanding of the function and regulation of most contact sites. To systematically characterize contact site proteomes, we established a high-throughput screening approach in Saccharomyces cerevisiae based on co-localization imaging. We imaged split fluorescence reporters for six different contact sites, several of which are poorly characterized, on the background of 1165 strains expressing a mCherry-tagged yeast protein that has a cellular punctate distribution (a hallmark of contact sites), under regulation of the strong TEF2 promoter. By scoring both co-localization events and effects on reporter size and abundance, we discovered over 100 new potential contact site residents and effectors in yeast. Focusing on several of the newly identified residents, we identified three homologs of Vps13 and Atg2 that are residents of multiple contact sites. These proteins share their lipid transport domain, thus expanding this family of lipid transporters. Analysis of another candidate, Ypr097w, which we now call Lec1 (Lipid-droplet Ergosterol Cortex 1), revealed that this previously uncharacterized protein dynamically shifts between lipid droplets and the cell cortex, and plays a role in regulation of ergosterol distribution in the cell. Overall, our analysis expands the universe of contact site residents and effectors and creates a rich database to mine for new functions, tethers, and regulators.
DOI der Erstveröffentlichung: 10.7554/eLife.74602
URL der Erstveröffentlichung: https://doi.org/10.7554/eLife.74602
Link zu diesem Datensatz: urn:nbn:de:bsz:291--ds-422310
hdl:20.500.11880/37916
http://dx.doi.org/10.22028/D291-42231
ISSN: 2050-084X
Datum des Eintrags: 21-Jun-2024
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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