Translational regulation of Pmt1 and Pmt2 by Bfr1 affects unfolded protein O-mannosylation
O-mannosylation is implicated in protein quality control in Saccharomyces cerevisiae due to the attachment of mannose to serine and threonine residues of un- or misfolded proteins in the endoplasmic reticulum (ER). This process also designated as unfolded protein O-mannosylation (UPOM) that ends fut...
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| Hauptverfasser: | , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
10 December 2019
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| In: |
International journal of molecular sciences
Year: 2019, Jahrgang: 20, Heft: 24 |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms20246220 |
| Online-Zugang: | Verlag, Volltext: https://doi.org/10.3390/ijms20246220 Verlag: https://www.mdpi.com/1422-0067/20/24/6220 
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| Verfasserangaben: | Joan Castells-Ballester, Natalie Rinis, Ilgin Kotan, Lihi Gal, Daniela Bausewein, Ilia Kats, Ewa Zatorska, Günter Kramer, Bernd Bukau, Maya Schuldiner and Sabine Strahl |
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| 245 | 1 | 0 | |a Translational regulation of Pmt1 and Pmt2 by Bfr1 affects unfolded protein O-mannosylation |c Joan Castells-Ballester, Natalie Rinis, Ilgin Kotan, Lihi Gal, Daniela Bausewein, Ilia Kats, Ewa Zatorska, Günter Kramer, Bernd Bukau, Maya Schuldiner and Sabine Strahl |
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| 500 | |a Name der Autorin "Natalie Rinis" ist in der Verfasserangabe falsch geschrieben | ||
| 520 | |a O-mannosylation is implicated in protein quality control in Saccharomyces cerevisiae due to the attachment of mannose to serine and threonine residues of un- or misfolded proteins in the endoplasmic reticulum (ER). This process also designated as unfolded protein O-mannosylation (UPOM) that ends futile folding cycles and saves cellular resources is mainly mediated by protein O-mannosyltransferases Pmt1 and Pmt2. Here we describe a genetic screen for factors that influence O-mannosylation in yeast, using slow-folding green fluorescent protein (GFP) as a reporter. Our screening identifies the RNA binding protein brefeldin A resistance factor 1 (Bfr1) that has not been linked to O-mannosylation and ER protein quality control before. We find that Bfr1 affects O-mannosylation through changes in Pmt1 and Pmt2 protein abundance but has no effect on PMT1 and PMT2 transcript levels, mRNA localization to the ER membrane or protein stability. Ribosome profiling reveals that Bfr1 is a crucial factor for Pmt1 and Pmt2 translation thereby affecting unfolded protein O-mannosylation. Our results uncover a new level of regulation of protein quality control in the secretory pathway. | ||
| 650 | 4 | |a Bfr1 | |
| 650 | 4 | |a endoplasmic reticulum | |
| 650 | 4 | |a mannosyltransferase | |
| 650 | 4 | |a O-mannosylation | |
| 650 | 4 | |a Pmt | |
| 650 | 4 | |a protein quality control | |
| 650 | 4 | |a RNA binding | |
| 650 | 4 | |a translation | |
| 650 | 4 | |a UPOM | |
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| 773 | 1 | 8 | |g volume:20 |g year:2019 |g number:24 |g extent:27 |a Translational regulation of Pmt1 and Pmt2 by Bfr1 affects unfolded protein O-mannosylation |
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