| |  Online-Ressource |
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| Verfasst von: | Castells Ballester, Joan [VerfasserIn]  |
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| | Zatorska, Ewa [VerfasserIn] |
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| | Meurer, Matthias [VerfasserIn] |
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| | Neubert, Patrick [VerfasserIn] |
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| | Metschies, Anke [VerfasserIn] |
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| | Knop, Michael [VerfasserIn] |
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| | Strahl, Sabine [VerfasserIn] |
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| Titel: | Monitoring protein dynamics in protein O-mannosyltransferase mutants in vivo by tandem fluorescent protein timers |
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| Verf.angabe: | Joan Castells-Ballester, Ewa Zatorska, Matthias Meurer, Patrick Neubert, Anke Metschies, Michael Knop, Sabine Strahl |
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| E-Jahr: | 2018 |
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| Jahr: | 12 October 2018 |
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| Umfang: | 10 S. |
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| Illustrationen: | Illustrationen |
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| Fussnoten: | Gesehen am 02.04.2019 |
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| Titel Quelle: | Enthalten in: Molecules |
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| Ort Quelle: | Basel : MDPI, 1996 |
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| Jahr Quelle: | 2018 |
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| Band/Heft Quelle: | volume 23, issue 10 (2018) Artikel-Nummer 2622, Seite 1-15, 15 Seiten |
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| ISSN Quelle: | 1420-3049 |
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| Abstract: | For proteins entering the secretory pathway, a major factor contributing to maturation and homeostasis is glycosylation. One relevant type of protein glycosylation is O-mannosylation, which is essential and evolutionarily-conserved in fungi, animals, and humans. Our recent proteome-wide study in the eukaryotic model organism Saccharomyces cerevisiae revealed that more than 26% of all proteins entering the secretory pathway receive O-mannosyl glycans. In a first attempt to understand the impact of O-mannosylation on these proteins, we took advantage of a tandem fluorescent timer (tFT) reporter to monitor different aspects of protein dynamics. We analyzed tFT-reporter fusions of 137 unique O-mannosylated proteins, mainly of the secretory pathway and the plasma membrane, in mutants lacking the major protein O-mannosyltransferases Pmt1, Pmt2, or Pmt4. In these three pmtΔ mutants, a total of 39 individual proteins were clearly affected, and Pmt-specific substrate proteins could be identified. We observed that O-mannosylation may cause both enhanced and diminished protein abundance and/or stability when compromised, and verified our findings on the examples of Axl2-tFT and Kre6-tFT fusion proteins. The identified target proteins are a valuable resource towards unraveling the multiple functions of O-mannosylation at the molecular level. |
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| DOI: | doi:10.3390/molecules23102622 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.3390/molecules23102622 |
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| | Volltext: https://www.mdpi.com/1420-3049/23/10/2622 |
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| | DOI: https://doi.org/10.3390/molecules23102622 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | <i>O</i>-mannosyl glycans |
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| | <i>Saccharomyces cerevisiae</i> |
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| | fluorescent protein timers |
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| | glycosylation |
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| | mannosyltransferase |
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| | PMT1 |
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| | PMT2 |
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| | PMT4 |
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| | protein turnover |
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| | secretory pathway |
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| | yeast |
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| K10plus-PPN: | 1662683774 |
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| Verknüpfungen: | → Zeitschrift |
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Monitoring protein dynamics in protein O-mannosyltransferase mutants in vivo by tandem fluorescent protein timers / Castells Ballester, Joan [VerfasserIn]; 12 October 2018 (Online-Ressource)
