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Cellular consequences of diminished protein O-Mannosyltransferase activity in baker’s yeast
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| Veröffentlicht in: | International journal of molecular sciences 18(2017,6) Artikel-Nummer 1226, 18 Seiten |
|---|---|
| Personen und Körperschaften: | , , , |
| Titel: | Cellular consequences of diminished protein O-Mannosyltransferase activity in baker’s yeast/ Ewa Zatorska, Lihi Gal, Jaro Schmitt, Daniela Bausewein, Maya Schuldiner and Sabine Strahl |
| Format: | E-Book-Kapitel |
| Sprache: | Englisch |
| veröffentlicht: |
9 June 2017
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| Gesamtaufnahme: |
: International journal of molecular sciences, 18(2017,6) Artikel-Nummer 1226, 18 Seiten
, volume:18 |
| Schlagwörter: | |
| Quelle: | Verbunddaten SWB Lizenzfreie Online-Ressourcen |
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| 245 | 1 | 0 | |a Cellular consequences of diminished protein O-Mannosyltransferase activity in baker’s yeast |c Ewa Zatorska, Lihi Gal, Jaro Schmitt, Daniela Bausewein, Maya Schuldiner and Sabine Strahl |
| 264 | 1 | |c 9 June 2017 | |
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| 520 | |a O-Mannosylation is a type of protein glycosylation initiated in the endoplasmic reticulum (ER) by the protein O-mannosyltransferase (PMT) family. Despite the vital role of O-mannosylation, its molecular functions and regulation are not fully characterized. To further explore the cellular impact of protein O-mannosylation, we performed a genome-wide screen to identify Saccharomyces cerevisiae mutants with increased sensitivity towards the PMT-specific inhibitor compound R3A-5a. We identified the cell wall and the ER as the cell compartments affected most upon PMT inhibition. Especially mutants with defects in N-glycosylation, biosynthesis of glycosylphosphatidylinositol-anchored proteins and cell wall β-1,6-glucan showed impaired growth when O-mannosylation became limiting. Signaling pathways that counteract cell wall defects and unbalanced ER homeostasis, namely the cell wall integrity pathway and the unfolded protein response, were highly crucial for the cell growth. Moreover, among the most affected mutants, we identified Ost3, one of two homologous subunits of the oligosaccharyltransferase complexes involved in N-glycosylation, suggesting a functional link between the two pathways. Indeed, we identified Pmt2 as a substrate for Ost3 suggesting that the reduced function of Pmt2 in the absence of N-glycosylation promoted sensitivity to the drug. Interestingly, even though S. cerevisiae Pmt1 and Pmt2 proteins are highly similar on the sequence, as well as the structural level and act as a complex, we identified only Pmt2, but not Pmt1, as an Ost3-specific substrate protein. | ||
| 650 | 4 | |a calcineurin | |
| 650 | 4 | |a cell wall | |
| 650 | 4 | |a endoplasmic reticulum | |
| 650 | 4 | |a glycosylation | |
| 650 | 4 | |a GPI anchor | |
| 650 | 4 | |a mannosyltransferase | |
| 650 | 4 | |a oligosaccharyltransferase | |
| 650 | 4 | |a unfolded protein response | |
| 700 | 1 | |a Schmitt, Jaro |e VerfasserIn |0 (DE-588)1167738209 |0 (DE-627)1031258027 |0 (DE-576)511249543 |4 aut | |
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| 700 | 1 | |a Strahl, Sabine |e VerfasserIn |0 (DE-588)1034793055 |0 (DE-627)74629073X |0 (DE-576)382427939 |4 aut | |
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| author | Zatorska, Ewa, Schmitt, Jaro, Bausewein, Daniela, Strahl, Sabine |
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| contents | O-Mannosylation is a type of protein glycosylation initiated in the endoplasmic reticulum (ER) by the protein O-mannosyltransferase (PMT) family. Despite the vital role of O-mannosylation, its molecular functions and regulation are not fully characterized. To further explore the cellular impact of protein O-mannosylation, we performed a genome-wide screen to identify Saccharomyces cerevisiae mutants with increased sensitivity towards the PMT-specific inhibitor compound R3A-5a. We identified the cell wall and the ER as the cell compartments affected most upon PMT inhibition. Especially mutants with defects in N-glycosylation, biosynthesis of glycosylphosphatidylinositol-anchored proteins and cell wall β-1,6-glucan showed impaired growth when O-mannosylation became limiting. Signaling pathways that counteract cell wall defects and unbalanced ER homeostasis, namely the cell wall integrity pathway and the unfolded protein response, were highly crucial for the cell growth. Moreover, among the most affected mutants, we identified Ost3, one of two homologous subunits of the oligosaccharyltransferase complexes involved in N-glycosylation, suggesting a functional link between the two pathways. Indeed, we identified Pmt2 as a substrate for Ost3 suggesting that the reduced function of Pmt2 in the absence of N-glycosylation promoted sensitivity to the drug. Interestingly, even though S. cerevisiae Pmt1 and Pmt2 proteins are highly similar on the sequence, as well as the structural level and act as a complex, we identified only Pmt2, but not Pmt1, as an Ost3-specific substrate protein. |
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| spelling | Zatorska, Ewa VerfasserIn (DE-588)1135603057 (DE-627)890522359 (DE-576)48987309X aut, Cellular consequences of diminished protein O-Mannosyltransferase activity in baker’s yeast Ewa Zatorska, Lihi Gal, Jaro Schmitt, Daniela Bausewein, Maya Schuldiner and Sabine Strahl, 9 June 2017, 18, Text txt rdacontent, Computermedien c rdamedia, Online-Ressource cr rdacarrier, Gesehen am 24.09.2018, O-Mannosylation is a type of protein glycosylation initiated in the endoplasmic reticulum (ER) by the protein O-mannosyltransferase (PMT) family. Despite the vital role of O-mannosylation, its molecular functions and regulation are not fully characterized. To further explore the cellular impact of protein O-mannosylation, we performed a genome-wide screen to identify Saccharomyces cerevisiae mutants with increased sensitivity towards the PMT-specific inhibitor compound R3A-5a. We identified the cell wall and the ER as the cell compartments affected most upon PMT inhibition. Especially mutants with defects in N-glycosylation, biosynthesis of glycosylphosphatidylinositol-anchored proteins and cell wall β-1,6-glucan showed impaired growth when O-mannosylation became limiting. Signaling pathways that counteract cell wall defects and unbalanced ER homeostasis, namely the cell wall integrity pathway and the unfolded protein response, were highly crucial for the cell growth. Moreover, among the most affected mutants, we identified Ost3, one of two homologous subunits of the oligosaccharyltransferase complexes involved in N-glycosylation, suggesting a functional link between the two pathways. Indeed, we identified Pmt2 as a substrate for Ost3 suggesting that the reduced function of Pmt2 in the absence of N-glycosylation promoted sensitivity to the drug. Interestingly, even though S. cerevisiae Pmt1 and Pmt2 proteins are highly similar on the sequence, as well as the structural level and act as a complex, we identified only Pmt2, but not Pmt1, as an Ost3-specific substrate protein., calcineurin, cell wall, endoplasmic reticulum, glycosylation, GPI anchor, mannosyltransferase, oligosaccharyltransferase, unfolded protein response, Schmitt, Jaro VerfasserIn (DE-588)1167738209 (DE-627)1031258027 (DE-576)511249543 aut, Bausewein, Daniela VerfasserIn (DE-588)1058663100 (DE-627)797375902 (DE-576)414813383 aut, Strahl, Sabine VerfasserIn (DE-588)1034793055 (DE-627)74629073X (DE-576)382427939 aut, Enthalten in International journal of molecular sciences Basel : Molecular Diversity Preservation International, 2000 18(2017,6) Artikel-Nummer 1226, 18 Seiten Online-Ressource (DE-627)316340715 (DE-600)2019364-6 (DE-576)281194653 1422-0067 nnns, volume:18 year:2017 number:6 extent:18, http://dx.doi.org/10.3390/ijms18061226 Verlag Resolving-System kostenfrei Volltext, https://www.mdpi.com/1422-0067/18/6/1226 Verlag kostenfrei Volltext, http://dx.doi.org/10.3390/ijms18061226 LFER, LFER 2018-10-10T00:00:00Z |
| spellingShingle | Zatorska, Ewa, Schmitt, Jaro, Bausewein, Daniela, Strahl, Sabine, Cellular consequences of diminished protein O-Mannosyltransferase activity in baker’s yeast, O-Mannosylation is a type of protein glycosylation initiated in the endoplasmic reticulum (ER) by the protein O-mannosyltransferase (PMT) family. Despite the vital role of O-mannosylation, its molecular functions and regulation are not fully characterized. To further explore the cellular impact of protein O-mannosylation, we performed a genome-wide screen to identify Saccharomyces cerevisiae mutants with increased sensitivity towards the PMT-specific inhibitor compound R3A-5a. We identified the cell wall and the ER as the cell compartments affected most upon PMT inhibition. Especially mutants with defects in N-glycosylation, biosynthesis of glycosylphosphatidylinositol-anchored proteins and cell wall β-1,6-glucan showed impaired growth when O-mannosylation became limiting. Signaling pathways that counteract cell wall defects and unbalanced ER homeostasis, namely the cell wall integrity pathway and the unfolded protein response, were highly crucial for the cell growth. Moreover, among the most affected mutants, we identified Ost3, one of two homologous subunits of the oligosaccharyltransferase complexes involved in N-glycosylation, suggesting a functional link between the two pathways. Indeed, we identified Pmt2 as a substrate for Ost3 suggesting that the reduced function of Pmt2 in the absence of N-glycosylation promoted sensitivity to the drug. Interestingly, even though S. cerevisiae Pmt1 and Pmt2 proteins are highly similar on the sequence, as well as the structural level and act as a complex, we identified only Pmt2, but not Pmt1, as an Ost3-specific substrate protein., calcineurin, cell wall, endoplasmic reticulum, glycosylation, GPI anchor, mannosyltransferase, oligosaccharyltransferase, unfolded protein response |
| swb_id_str | 511250770 |
| title | Cellular consequences of diminished protein O-Mannosyltransferase activity in baker’s yeast |
| title_auth | Cellular consequences of diminished protein O-Mannosyltransferase activity in baker’s yeast |
| title_full | Cellular consequences of diminished protein O-Mannosyltransferase activity in baker’s yeast Ewa Zatorska, Lihi Gal, Jaro Schmitt, Daniela Bausewein, Maya Schuldiner and Sabine Strahl |
| title_fullStr | Cellular consequences of diminished protein O-Mannosyltransferase activity in baker’s yeast Ewa Zatorska, Lihi Gal, Jaro Schmitt, Daniela Bausewein, Maya Schuldiner and Sabine Strahl |
| title_full_unstemmed | Cellular consequences of diminished protein O-Mannosyltransferase activity in baker’s yeast Ewa Zatorska, Lihi Gal, Jaro Schmitt, Daniela Bausewein, Maya Schuldiner and Sabine Strahl |
| title_in_hierarchy | Cellular consequences of diminished protein O-Mannosyltransferase activity in baker’s yeast / Ewa Zatorska, Lihi Gal, Jaro Schmitt, Daniela Bausewein, Maya Schuldiner and Sabine Strahl, |
| title_short | Cellular consequences of diminished protein O-Mannosyltransferase activity in baker’s yeast |
| title_sort | cellular consequences of diminished protein o mannosyltransferase activity in baker s yeast |
| topic | calcineurin, cell wall, endoplasmic reticulum, glycosylation, GPI anchor, mannosyltransferase, oligosaccharyltransferase, unfolded protein response |
| topic_facet | calcineurin, cell wall, endoplasmic reticulum, glycosylation, GPI anchor, mannosyltransferase, oligosaccharyltransferase, unfolded protein response |
| url | http://dx.doi.org/10.3390/ijms18061226, https://www.mdpi.com/1422-0067/18/6/1226 |