ArticleMolecular immunology2019
A nanobody that recognizes a 14-residue peptide epitope in the E2 ubiquitin-conjugating enzyme UBC6e modulates its activity.
Article in Molecular immunology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 51 citations in OpenAlex.
- Antigen-Detected NMR for Minimal Epitope Engineering and Structure-Guided Selection of a NaAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Nanobody-Based Bioconjugates as Potent and Broadly Active Inhibitors of HIV Entry.Journal of the American Chemical Society · 2026Article
- Development of bitopic nanobody-ligand conjugates targeting G protein-coupled receptors and exhibiting logic-gated signaling.PLoS biology · 2025Article
- CD45 sequestration lowers the signaling threshold in lymphocytes and enhances anti-tumor immunity.bioRxiv : the preprint server for biology · 2025Article
- Evaluation of AlphaFold modeling for elucidation of nanobody-peptide epitope interactions.The Journal of biological chemistry · 2025Article
- Genetically encoded affinity reagents are a toolkit for visualizing and manipulating endogenous protein function in vivo.Nature communications · 2025Article
- A nanobody that binds to the backside of the ubiquitin conjugating enzyme Ube2G2 differentially affects interactions with its partner E3 Ligases.Communications biology · 2025Article
- Generation of Site-Specifically Labeled Affinity Reagents via Use of a Self-Labeling Single Domain Antibody.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Evaluation of Alphafold modeling for elucidation of nanobody-peptide epitope interactions.bioRxiv : the preprint server for biology · 2025Article
- Nanobody-based conjugates targeting small molecule-binding GPCRs and exhibiting logic-gated signaling.bioRxiv : the preprint server for biology · 2025Article
- Recombinant venom proteins in insect seminal fluid reduce female lifespan.Nature communications · 2025Article
- Chemically Induced Dimerization via Nanobody Binding Facilitates in Situ Ligand Assembly and On-Demand GPCR Activation.JACS Au · 2024Article
- Repurposing a plant peptide cyclase for targeted lysine acylation.Nature chemistry · 2024Article
- Nanobody-Mediated Dualsteric Engagement of the Angiotensin Receptor Broadens Biased Ligand Pharmacology.Molecular pharmacology · 2024Article
- Semi-synthetic nanobody-ligand conjugates exhibit tunable signaling properties and enhanced transcriptional outputs at neurokinin receptor-1.Protein science : a publication of the Protein Society · 2024Article
- Production of recombinant HPV11/16 E6/E7-MBP-HisVirology journal · 2024Article
- Semi-synthetic nanobody-ligand conjugates exhibit tunable signaling properties and enhanced transcriptional outputs at neurokinin receptor-1.bioRxiv : the preprint server for biology · 2023Article
- Characterization ofFrontiers in immunology · 2023Article
- NanoTag Nanobody Tools for Drosophila In Vitro and In Vivo Studies.Current protocols · 2022Article
- Rapid Covalent Labeling of Membrane Proteins on Living Cells Using a Nanobody-Epitope Tag Pair.Bioconjugate chemistry · 2022Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
A substantial fraction of eukaryotic proteins is folded and modified in the endoplasmic reticulum (ER) prior to export and secretion. Proteins that enter the ER but fail to fold correctly must be degraded, mostly in a process termed ER-associated degradation (ERAD). Both protein folding in the ER and ERAD are essential for proper immune function. Several E2 and E3 enzymes localize to the ER and are essential for various aspects of ERAD, but their functions and regulation are incompletely understood. Here we identify and characterize single domain antibody fragments derived from the variable domain of alpaca heavy chain-only antibodies (VHHs or nanobodies) that bind to the ER-localized E2 UBC6e, an enzyme implicated in ERAD. One such VHH, VHH05 recognizes a 14 residue stretch and enhances the rate of E1-catalyzed ubiquitin E2 loading in vitroand interferes with phosphorylation of UBC6e in response to cell stress. Identification of the peptide epitope recognized by VHH05 places it outside the E2 catalytic core, close to the position of activation-induced phosphorylation on Ser184. Our data thus suggests a site involved in allosteric regulation of UBC6e's activity. This VHH should be useful not only to dissect the participation of UBC6e in ERAD and in response to cell stress, but also as a high affinity epitope tag-specific reagent of more general utility.
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