Protein O-mannosylation in the early secretory pathway
Protein O-mannosylation and N-glycosylation are essential post-translational modifications, which initiate in the endoplasmic reticulum (ER). In yeast, the two glycosylation machineries act at the Sec61 translocon complex where they can even compete for certain substrate proteins. N-linked glycans p...
Gespeichert in:
| Hauptverfasser: | , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
7th May 2016
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| In: |
Current opinion in cell biology
Year: 2016, Jahrgang: 41, Pages: 100-108 |
| ISSN: | 1879-0410 |
| DOI: | 10.1016/j.ceb.2016.04.010 |
| Online-Zugang: | Verlag, Volltext: http://dx.doi.org/10.1016/j.ceb.2016.04.010 Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S0955067416300850 
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| Verfasserangaben: | Patrick Neubert and Sabine Strahl |
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| 520 | |a Protein O-mannosylation and N-glycosylation are essential post-translational modifications, which initiate in the endoplasmic reticulum (ER). In yeast, the two glycosylation machineries act at the Sec61 translocon complex where they can even compete for certain substrate proteins. N-linked glycans play a crucial role in the ER quality control of glycoproteins. In recent years, it became clear that in addition to its important functions for cell surface proteins, O-mannosylation impacts the ER protein homeostasis. These glycans can exclude unfavorable folding intermediates from futile folding attempts, increase the solubility of irreversibly misfolded proteins, and even mark them for degradation. O-Mannose glycoproteomics now captures the molecular complexity of this modification opening exciting opportunities to explore further roles of O-mannosylation in the early secretory pathway. | ||
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