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doi:10.22028/D291-42231
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 |
Dateien zu diesem Datensatz:
Datei | Beschreibung | Größe | Format | |
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elife-74602-v1.pdf | 8,23 MB | Adobe PDF | Öffnen/Anzeigen |
Diese Ressource wurde unter folgender Copyright-Bestimmung veröffentlicht: Lizenz von Creative Commons