Purified EDEM3 or EDEM1 alone produces determinant oligosaccharide structures from M8B in mammalian glycoprotein ERAD
Sequential mannose trimming of N-glycan, from M9 to M8B and then to oligosaccharides exposing the α1,6-linked mannosyl residue (M7A, M6, and M5), facilitates endoplasmic reticulum-associated degradation of misfolded glycoproteins (gpERAD). We previously showed that EDEM2 stably disulfide-bonded to t...
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eLife Sciences Publications Ltd
2021
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oai:doaj.org-article:341ffd41c9234c5d998d7ae1195a462d2021-11-05T17:50:57ZPurified EDEM3 or EDEM1 alone produces determinant oligosaccharide structures from M8B in mammalian glycoprotein ERAD10.7554/eLife.703572050-084Xe70357https://doaj.org/article/341ffd41c9234c5d998d7ae1195a462d2021-10-01T00:00:00Zhttps://elifesciences.org/articles/70357https://doaj.org/toc/2050-084XSequential mannose trimming of N-glycan, from M9 to M8B and then to oligosaccharides exposing the α1,6-linked mannosyl residue (M7A, M6, and M5), facilitates endoplasmic reticulum-associated degradation of misfolded glycoproteins (gpERAD). We previously showed that EDEM2 stably disulfide-bonded to the thioredoxin domain-containing protein TXNDC11 is responsible for the first step (George et al., 2020). Here, we show that EDEM3 and EDEM1 are responsible for the second step. Incubation of pyridylamine-labeled M8B with purified EDEM3 alone produced M7 (M7A and M7C), M6, and M5. EDEM1 showed a similar tendency, although much lower amounts of M6 and M5 were produced. Thus, EDEM3 is a major α1,2-mannosidase for the second step from M8B. Both EDEM3 and EDEM1 trimmed M8B from a glycoprotein efficiently. Our confirmation of the Golgi localization of MAN1B indicates that no other α1,2-mannosidase is required for gpERAD. Accordingly, we have established the entire route of oligosaccharide processing and the enzymes responsible.Ginto GeorgeSatoshi NinagawaHirokazu YagiJun-ichi FurukawaNoritaka HashiiAkiko Ishii-WatabeYing DengKazutoshi MatsushitaTokiro IshikawaYugoviandi P MamahitYuta MakiYasuhiro KajiharaKoichi KatoTetsuya OkadaKazutoshi MorieLife Sciences Publications Ltdarticleprotein degradationglycoproteinmannose trimmingMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021) |
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DOAJ |
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| topic |
protein degradation glycoprotein mannose trimming Medicine R Science Q Biology (General) QH301-705.5 |
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protein degradation glycoprotein mannose trimming Medicine R Science Q Biology (General) QH301-705.5 Ginto George Satoshi Ninagawa Hirokazu Yagi Jun-ichi Furukawa Noritaka Hashii Akiko Ishii-Watabe Ying Deng Kazutoshi Matsushita Tokiro Ishikawa Yugoviandi P Mamahit Yuta Maki Yasuhiro Kajihara Koichi Kato Tetsuya Okada Kazutoshi Mori Purified EDEM3 or EDEM1 alone produces determinant oligosaccharide structures from M8B in mammalian glycoprotein ERAD |
| description |
Sequential mannose trimming of N-glycan, from M9 to M8B and then to oligosaccharides exposing the α1,6-linked mannosyl residue (M7A, M6, and M5), facilitates endoplasmic reticulum-associated degradation of misfolded glycoproteins (gpERAD). We previously showed that EDEM2 stably disulfide-bonded to the thioredoxin domain-containing protein TXNDC11 is responsible for the first step (George et al., 2020). Here, we show that EDEM3 and EDEM1 are responsible for the second step. Incubation of pyridylamine-labeled M8B with purified EDEM3 alone produced M7 (M7A and M7C), M6, and M5. EDEM1 showed a similar tendency, although much lower amounts of M6 and M5 were produced. Thus, EDEM3 is a major α1,2-mannosidase for the second step from M8B. Both EDEM3 and EDEM1 trimmed M8B from a glycoprotein efficiently. Our confirmation of the Golgi localization of MAN1B indicates that no other α1,2-mannosidase is required for gpERAD. Accordingly, we have established the entire route of oligosaccharide processing and the enzymes responsible. |
| format |
article |
| author |
Ginto George Satoshi Ninagawa Hirokazu Yagi Jun-ichi Furukawa Noritaka Hashii Akiko Ishii-Watabe Ying Deng Kazutoshi Matsushita Tokiro Ishikawa Yugoviandi P Mamahit Yuta Maki Yasuhiro Kajihara Koichi Kato Tetsuya Okada Kazutoshi Mori |
| author_facet |
Ginto George Satoshi Ninagawa Hirokazu Yagi Jun-ichi Furukawa Noritaka Hashii Akiko Ishii-Watabe Ying Deng Kazutoshi Matsushita Tokiro Ishikawa Yugoviandi P Mamahit Yuta Maki Yasuhiro Kajihara Koichi Kato Tetsuya Okada Kazutoshi Mori |
| author_sort |
Ginto George |
| title |
Purified EDEM3 or EDEM1 alone produces determinant oligosaccharide structures from M8B in mammalian glycoprotein ERAD |
| title_short |
Purified EDEM3 or EDEM1 alone produces determinant oligosaccharide structures from M8B in mammalian glycoprotein ERAD |
| title_full |
Purified EDEM3 or EDEM1 alone produces determinant oligosaccharide structures from M8B in mammalian glycoprotein ERAD |
| title_fullStr |
Purified EDEM3 or EDEM1 alone produces determinant oligosaccharide structures from M8B in mammalian glycoprotein ERAD |
| title_full_unstemmed |
Purified EDEM3 or EDEM1 alone produces determinant oligosaccharide structures from M8B in mammalian glycoprotein ERAD |
| title_sort |
purified edem3 or edem1 alone produces determinant oligosaccharide structures from m8b in mammalian glycoprotein erad |
| publisher |
eLife Sciences Publications Ltd |
| publishDate |
2021 |
| url |
https://doaj.org/article/341ffd41c9234c5d998d7ae1195a462d |
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