ArticleThe Plant journal : for cell and molecular biology2014
The transmembrane domain of N -acetylglucosaminyltransferase I is the key determinant for its Golgi subcompartmentation.
Article in The Plant journal : for cell and molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 26 citations in OpenAlex.
- Interaction with COPII Member SAR1 Is Critical for the Delivery ofPlants (Basel, Switzerland) · 2026Article
- 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
- Elucidation of the late steps in the glycan-dependent ERAD of soluble misfolded glycoproteins.The Plant journal : for cell and molecular biology · 2025Article
- Analysis of Protein Glycosylation in the ER.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The tobacco GNTI stem region harbors a strong motif for homomeric protein complex formation.Frontiers in plant science · 2023Article
- Critical Determinants in ER-Golgi Trafficking of Enzymes Involved in Glycosylation.Plants (Basel, Switzerland) · 2022Review
- On the nature of the plant ER exit sites.Frontiers in plant science · 2022Article
- Inactivation ofFrontiers in plant science · 2021Article
- Functional characterization of Schistosoma mansoni fucosyltransferases in Nicotiana benthamiana plants.Scientific reports · 2020Article
- BGAL1 depletion boosts the level of β-galactosylation of N- and O-glycans in N. benthamiana.Plant biotechnology journal · 2020Article
- A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD.Nature communications · 2019Article
- The Golgi Localization of GnTI Requires a Polar Amino Acid Residue within Its Transmembrane Domain.Plant physiology · 2019Article
- The glycan-dependent ERAD machinery degrades topologically diverse misfolded proteins.The Plant journal : for cell and molecular biology · 2018Article
- Processing of the Terminal Alpha-1,2-Linked Mannose Residues From OligomannosidicFrontiers in plant science · 2018Article
- Analysis of Protein Glycosylation in the ER.Methods in molecular biology (Clifton, N.J.) · 2018Article
- N-Glycosylation of an IgG antibody secreted by Nicotiana tabacum BY-2 cells can be modulated through co-expression of human β-1,4-galactosyltransferase.Transgenic research · 2017Article
- Reduced paucimannosidic N-glycan formation by suppression of a specific β-hexosaminidase from Nicotiana benthamiana.Plant biotechnology journal · 2017Article
- Plant protein glycosylation.Glycobiology · 2016Review
- Characterization of plants expressing the human β1,4-galactosyltrasferase gene.Plant physiology and biochemistry : PPB · 2015Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Golgi-resident type-II membrane proteins are asymmetrically distributed across the Golgi stack. The intrinsic features of the protein that determine its subcompartment-specific concentration are still largely unknown. Here, we used a series of chimeric proteins to investigate the contribution of the cytoplasmic, transmembrane and stem region of Nicotiana benthamiana N-acetylglucosaminyltransferase I (GnTI) for its cis/medial-Golgi localization and for protein-protein interaction in the Golgi. The individual GnTI protein domains were replaced with those from the well-known trans-Golgi enzyme α2,6-sialyltransferase (ST) and transiently expressed in Nicotiana benthamiana. Using co-localization analysis and N-glycan profiling, we show that the transmembrane domain of GnTI is the major determinant for its cis/medial-Golgi localization. By contrast, the stem region of GnTI contributes predominately to homomeric and heteromeric protein complex formation. Importantly, in transgenic Arabidopsis thaliana, a chimeric GnTI variant with altered sub-Golgi localization was not able to complement the GnTI-dependent glycosylation defect. Our results suggest that sequence-specific features in the transmembrane domain of GnTI account for its steady-state distribution in the cis/medial-Golgi in plants, which is a prerequisite for efficient N-glycan processing in vivo.
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