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EDEM2 stably disulfide-bonded to TXNDC11 catalyzes the first mannose trimming step in mammalian glycoprotein ERAD
Bibliographic Information
- Other Title
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- EDEM2 stable disulfide-bonded to TXNDC11 catalyzes the first mannose trimming step in mammalian glycoprotein ERAD
Description
Sequential mannose trimming of N-glycan (Man9GlcNAc2 -> Man8GlcNAc2 -> Man7GlcNAc2) facilitates endoplasmic reticulum-associated degradation of misfolded glycoproteins (gpERAD). Our gene knockout experiments in human HCT116 cells have revealed that EDEM2 is required for the first step. However, it was previously shown that purified EDEM2 exhibited no α1, 2-mannosidase activity toward Man9GlcNAc2 in vitro. Here, we found that EDEM2 was stably disulfide-bonded to TXNDC11, an endoplasmic reticulum protein containing five thioredoxin (Trx)-like domains. C558 present outside of the mannosidase homology domain of EDEM2 was linked to C692 in Trx5, which solely contains the CXXC motif in TXNDC11. This covalent bonding was essential for mannose trimming and subsequent gpERAD in HCT116 cells. Furthermore, EDEM2-TXNDC11 complex purified from transfected HCT116 cells converted Man9GlcNAc2 to Man8GlcNAc2(isomerB) in vitro. Our results establish the role of EDEM2 as an initiator of gpERAD, and represent the first clear demonstration of in vitro mannosidase activity of EDEM family proteins.
Journal
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- eLife
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eLife 9 e53455-, 2020-02-17
eLife Sciences Publications, Ltd
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Keywords
- glycoprotein
- QH301-705.5
- Science
- Polymerase Chain Reaction
- Catalysis
- alpha-Mannosidase
- CRISPR-Associated Protein 9
- Mannosidases
- Humans
- protein misfolding
- Biology (General)
- Glycoproteins
- Gene Editing
- Q
- R
- Cell Biology
- Endoplasmic Reticulum-Associated Degradation
- HCT116 Cells
- endoplasmic reticulum
- mannose trimming
- Gene Knockdown Techniques
- protein degradation
- Medicine
- CRISPR-Cas Systems
- Carrier Proteins
- Mannose
Details 詳細情報について
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- CRID
- 1050846638692947712
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- NII Article ID
- 120006817590
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- ISSN
- 2050084X
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- HANDLE
- 2433/246428
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- PubMed
- 32065582
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- Text Lang
- en
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- Article Type
- journal article
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- Data Source
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- IRDB
- Crossref
- CiNii Articles
- KAKEN
- OpenAIRE