ArticleThe Plant cell2006
Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway.
Article in The Plant cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.
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Who cites it
111 citing papers in PubMed, 208 citations in OpenAlex.
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- Xyloglucan Endotransglycosylase/Hydrolase Downregulation IncreasesInternational journal of molecular sciences · 2025Article
- Advances and challenges in plant N-glycoengineering: when fucosylation matters.Frontiers in plant science · 2025Review
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- CELLULOSE SYNTHASE-LIKE C proteins modulate cell wall establishment during ethylene-mediated root growth inhibition in rice.The Plant cell · 2024Article
- NKS1/ELMO4 is an integral protein of a pectin synthesis protein complex and maintains Golgi morphology and cell adhesion inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Establishment of an efficient cotton root protoplast isolation protocol suitable for single-cell RNA sequencing and transient gene expression analysis.Plant methods · 2023Article
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- A New Method for Rapid Subcellular Localization and Gene Function Analysis in Cotton Based on Barley Stripe Mosaic Virus.Plants (Basel, Switzerland) · 2022Article
- Critical Determinants in ER-Golgi Trafficking of Enzymes Involved in Glycosylation.Plants (Basel, Switzerland) · 2022Review
- Lectin affinity-based glycoproteome analysis of the developing xylem in poplar.Forestry research · 2022Article
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- A G protein-coupled receptor-like module regulates cellulose synthase secretion from the endomembrane system in Arabidopsis.Developmental cell · 2021Article
- BIG3 and BIG5 Redundantly Mediate Vesicle Trafficking inBiomolecules · 2021Article
- Actin and Microtubules Differently Contribute to Vacuolar Targeting Specificity during the Export from the ER.Membranes · 2021Article
- Organelle Visualization With Multicolored Fluorescent Markers in Bamboo.Frontiers in plant science · 2021Article
- Polysaccharide Biosynthesis: Glycosyltransferases and Their Complexes.Frontiers in plant science · 2021Article
- SUPER STARCHY1/ONAC025 participates in rice grain filling.Plant direct · 2020Article
51 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The processing of N-linked oligosaccharides in the secretory pathway requires the sequential action of a number of glycosidases and glycosyltransferases. We studied the spatial distribution of several type II membrane-bound enzymes from Glycine max, Arabidopsis thaliana, and Nicotiana tabacum. Glucosidase I (GCSI) localized to the endoplasmic reticulum (ER), alpha-1,2 mannosidase I (ManI) and N-acetylglucosaminyltransferase I (GNTI) both targeted to the ER and Golgi, and beta-1,2 xylosyltransferase localized exclusively to Golgi stacks, corresponding to the order of expected function. ManI deletion constructs revealed that the ManI transmembrane domain (TMD) contains all necessary targeting information. Likewise, GNTI truncations showed that this could apply to other type II enzymes. A green fluorescent protein chimera with ManI TMD, lengthened by duplicating its last seven amino acids, localized exclusively to the Golgi and colocalized with a trans-Golgi marker (ST52-mRFP), suggesting roles for protein-lipid interactions in ManI targeting. However, the TMD lengths of other plant glycosylation enzymes indicate that this mechanism cannot apply to all enzymes in the pathway. In fact, removal of the first 11 amino acids of the GCSI cytoplasmic tail resulted in relocalization from the ER to the Golgi, suggesting a targeting mechanism relying on protein-protein interactions. We conclude that the localization of N-glycan processing enzymes corresponds to an assembly line in the early secretory pathway and depends on both TMD length and signals in the cytoplasmic tail.
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