ArticleTraffic (Copenhagen, Denmark)2009
Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes.
Article in Traffic (Copenhagen, Denmark), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
58 citing papers in PubMed, 89 citations in OpenAlex.
- Interaction with COPII Member SAR1 Is Critical for the Delivery ofPlants (Basel, Switzerland) · 2026Article
- Multiprotein Complexes of Plant Glycosyltransferases Involved in Their Function and Trafficking.Plants (Basel, Switzerland) · 2025Review
- Elucidation of the late steps in the glycan-dependent ERAD of soluble misfolded glycoproteins.The Plant journal : for cell and molecular biology · 2025Article
- Trafficking and localization of Golgi-residentFrontiers in plant science · 2025Review
- Production andFrontiers in plant science · 2023Article
- The tobacco GNTI stem region harbors a strong motif for homomeric protein complex formation.Frontiers in plant science · 2023Article
- Article
- Critical Determinants in ER-Golgi Trafficking of Enzymes Involved in Glycosylation.Plants (Basel, Switzerland) · 2022Review
- Reteplase Fc-fusions produced in N. benthamiana are able to dissolve blood clots ex vivo.PloS one · 2021Article
- Polysaccharide Biosynthesis: Glycosyltransferases and Their Complexes.Frontiers in plant science · 2021Article
- Functional characterization of Schistosoma mansoni fucosyltransferases in Nicotiana benthamiana plants.Scientific reports · 2020Article
- Show me your secret(ed) weapons: a multifaceted approach reveals a wide arsenal of type III-secreted effectors in the cucurbit pathogenic bacterium Acidovorax citrulli and novel effectors in the Acidovorax genus.Molecular plant pathology · 2020Article
- The Crucial Role of Demannosylating Asparagine-Linked Glycans in ERADicating Misfolded Glycoproteins in the Endoplasmic Reticulum.Frontiers in plant science · 2020Review
- Development of a minigenome cassette for Lettuce necrotic yellows virus: A first step in rescuing a plant cytorhabdovirus.PloS one · 2020Article
- A conserved arginine/lysine-based motif promotes ER export of KCNE1 and KCNE2 to regulate KCNQ1 channel activity.Channels (Austin, Tex.) · 2019Article
- 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
- An oligosaccharyltransferase from Leishmania major increases the N-glycan occupancy on recombinant glycoproteins produced in Nicotiana benthamiana.Plant biotechnology journal · 2018Article
- Transport from the endoplasmic reticulum to the Golgi in plants: Where are we now?Seminars in cell & developmental biology · 2018Review
- The glycan-dependent ERAD machinery degrades topologically diverse misfolded proteins.The Plant journal : for cell and molecular biology · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Plant N-glycan processing enzymes are arranged along the early secretory pathway, forming an assembly line to facilitate the step-by-step modification of oligosaccharides on glycoproteins. Thus, these enzymes provide excellent tools to study signals and mechanisms, promoting their localization and retention in the endoplasmic reticulum (ER) and Golgi apparatus. Herein, we focused on a detailed investigation of amino acid sequence motifs present in their short cytoplasmic tails in respect to ER export. Using site-directed mutagenesis, we determined that single arginine/lysine residues within the cytoplasmic tail are sufficient to promote rapid Golgi targeting of Golgi-resident N-acetylglucosaminyltransferase I (GnTI) and alpha-mannosidase II (GMII). Furthermore, we reveal that an intact ER export motif is essential for proper in vivo function of GnTI. Coexpression studies with Sar1p provided evidence for COPII-dependent transport of GnTI to the Golgi. Our data provide evidence that efficient ER export of Golgi-resident plant N-glycan processing enzymes occurs through a selective mechanism based on recognition of single basic amino acids present in their cytoplasmic tails.
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What OpenQuestion holds
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.