ArticleNature communications2019
A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 37 citations in OpenAlex.
- Interaction with COPII Member SAR1 Is Critical for the Delivery ofPlants (Basel, Switzerland) · 2026Article
- Plant Golgi and GECCO: The Universality of ER-Golgi Interface.Sub-cellular biochemistry · 2026Review
- A plant cell-based platform for the expression of complex proteins with fucose-reduced sialylated N-glycans.Plant biotechnology journal · 2026Article
- Quantitative glycoproteomics identifies target N-glycoproteins of the Golgi-class I α-mannosidase SlMNSI1 that is important for tomato fruit development.Plant communications · 2025Article
- Suborganellar resolution imaging for the localisation of human glycosylation enzymes in tobacco Golgi bodies.Journal of microscopy · 2025Article
- Trafficking and localization of Golgi-residentFrontiers in plant science · 2025Review
- Reply to: Does the KDEL receptor cycle between the Golgi and the ER?Nature communications · 2024Article
- Analysis of Protein Glycosylation in the ER.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The K/HDEL receptor does not recycle but instead acts as a Golgi-gatekeeper.Nature communications · 2023Article
- Pseudomonas syringae DC3000 infection increases glucosylated N-glycans in Arabidopsis thaliana.Glycoconjugate journal · 2023Article
- An oligosaccharyltransferase fromFrontiers in plant science · 2023Article
- Article
- Article
- Transient Expression of Glycosylated SARS-CoV-2 Antigens inPlants (Basel, Switzerland) · 2022Review
- Critical Determinants in ER-Golgi Trafficking of Enzymes Involved in Glycosylation.Plants (Basel, Switzerland) · 2022Review
- A glossary of plant cell structures: Current insights and future questions.The Plant cell · 2022Review
- A Predominant Role of AtEDEM1 in Catalyzing a Rate-Limiting Demannosylation Step of an Arabidopsis Endoplasmic Reticulum-Associated Degradation Process.Frontiers in plant science · 2022Article
- A Non-redundant Function of MNS5: A Class I α-1, 2 Mannosidase, in the Regulation of Endoplasmic Reticulum-Associated Degradation of Misfolded Glycoproteins.Frontiers in plant science · 2022Article
- An Update on the Key Factors Required for Plant Golgi Structure Maintenance.Frontiers in plant science · 2022Review
- On the nature of the plant ER exit sites.Frontiers in plant science · 2022Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
The Arabidopsis ER-α-mannosidase I (MNS3) generates an oligomannosidic N-glycan structure that is characteristically found on ER-resident glycoproteins. The enzyme itself has so far not been detected in the ER. Here, we provide evidence that in plants MNS3 exclusively resides in the Golgi apparatus at steady-state. Notably, MNS3 remains on dispersed punctate structures when subjected to different approaches that commonly result in the relocation of Golgi enzymes to the ER. Responsible for this rare behavior is an amino acid signal motif (LPYS) within the cytoplasmic tail of MNS3 that acts as a specific Golgi retention signal. This retention is a means to spatially separate MNS3 from ER-localized mannose trimming steps that generate the glycan signal required for flagging terminally misfolded glycoproteins for ERAD. The physiological importance of the very specific MNS3 localization is demonstrated here by means of a structurally impaired variant of the brassinosteroid receptor BRASSINOSTEROID INSENSITIVE 1.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.