Protein O-mannosylation in the early secretory pathway

• Verfasst von: Neubert, Patrick [VerfasserIn]
• Verfasst von: Strahl, Sabine [VerfasserIn]
• Titel: Protein O-mannosylation in the early secretory pathway
• Verf.angabe: Patrick Neubert and Sabine Strahl
• E-Jahr: 2016
• Jahr: 7th May 2016
• Umfang: 9 S.
• Fussnoten: Gesehen am 10.05.2017
• Titel Quelle: Enthalten in: Current opinion in cell biology
• Ort Quelle: Amsterdam [u.a.] : Elsevier, 1989
• Jahr Quelle: 2016
• Band/Heft Quelle: 41(2016), Seite 100-108
• ISSN Quelle: 1879-0410
• DOI: doi:10.1016/j.ceb.2016.04.010
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1558379916

Abstract

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.