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. 2014 Mar;7(3):331–341. doi: 10.1242/dmm.014589

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© 2014. Published by The Company of Biologists Ltd

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.

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Fig. 3. — Glycoprotein ERAD. Degradation of terminally misfolded glycoproteins through ERAD is probably initiated by cleavage of the terminal B-chain mannose (green circles) of Man₉GlcNAc₂ (and possibly Glc₁Man₉GlcNAc₂) N-glycan forms by ER mannosidase I (ERManI, step 1). This results in the formation and recognition of this specific Man₈GlcNAc₂ form by ER-degradation-enhancing alpha-mannosidase-like 1 (EDEM1). Then, removal of the terminal C-chain mannose, either: (1) directly by EDEM3 or possibly Golgi mannosidase I (step 2), or (2) by highly concentrated ERMan I in the ERQC compartment (step 3), exposes an α1-6 linked mannose that is recognized by OS-9. OS-9 facilitates transport of the misfolded substrate to the core ERAD HRD1-SEL1L complex (step 4), and subsequent retrotranslocation to the cytoplasm for degradation by the proteasome (step 5).