ArticleNature chemical biology2016
Fluorogenic probes reveal a role of GLUT4 N-glycosylation in intracellular trafficking.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 52 citations in OpenAlex.
- Glycosylation modification: a trigger for obesity and its complications?Molecular medicine (Cambridge, Mass.) · 2026Review
- Controlling Intramolecular Rotation with Five-Membered Heterocycles Facilitates the Design of Highly Cell-Permeable Xanthene-Based Fluorogenic Probes.Journal of the American Chemical Society · 2025Article
- Non-invasive in vivo monitoring of PROTAC-mediated protein degradation using an environment-sensitive reporter.Nature communications · 2025Article
- Article
- Bioisostere-conjugated fluorescent probes for live-cell protein imaging without non-specific organelle accumulation.Chemical science · 2024Article
- Visualization of multiple localizations of GLUT4 by fluorescent probes of PYP-tag with designed unnatural warhead.Chemical science · 2023Article
- An "OFF-ON-OFF" fluorescence protein-labeling probe for real-time visualization of the degradation of short-lived proteins in cellular systems.Chemical science · 2022Article
- RNA-based cooperative protein labeling that permits direct monitoring of the intracellular concentration change of an endogenous protein.Nucleic acids research · 2021Article
- PD-L2 glycosylation promotes immune evasion and predicts anti-EGFR efficacy.Journal for immunotherapy of cancer · 2021Article
- A Palette of Minimally Tagged Sucrose Analogues for Real-Time Raman Imaging of Intracellular Plant Metabolism.Angewandte Chemie (International ed. in English) · 2021Article
- A Palette of Minimally Tagged Sucrose Analogues for Real-Time Raman Imaging of Intracellular Plant Metabolism.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Article
- Ligand-directed two-step labeling to quantify neuronal glutamate receptor trafficking.Nature communications · 2021Article
- Near-infrared fluorescent probes: a next-generation tool for protein-labeling applications.Chemical science · 2020Review
- Glucose transporters in adipose tissue, liver, and skeletal muscle in metabolic health and disease.Pflugers Archiv : European journal of physiology · 2020Review
- Article
- Rapid no-wash labeling of PYP-tag proteins with reactive fluorogenic ligands affords stable fluorescent protein conjugates for long-term cell imaging studies.Chemical science · 2020Article
- Next-Generation Fluorogen-Based Reporters and Biosensors for Advanced Bioimaging.International journal of molecular sciences · 2019Review
- Development of an effective protein-labeling system based on smart fluorogenic probes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Review
- SCOTfluors: Small, Conjugatable, Orthogonal, and Tunable Fluorophores for In Vivo Imaging of Cell Metabolism.Angewandte Chemie (International ed. in English) · 2019Article
- Quinone-Derived π-Extended Phenazines as New Fluorogenic Probes for Live-Cell Imaging of Lipid Droplets.Frontiers in chemistry · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glucose transporter 4 (GLUT4) is an N-glycosylated protein that maintains glucose homeostasis by regulating the protein translocation. To date, it has been unclear whether the N-glycan of GLUT4 contributes to its intracellular trafficking. Here, to clarify the role of the N-glycan, we developed fluorogenic probes that label cytoplasmic and plasma-membrane proteins for multicolor imaging of GLUT4 translocation. One of the probes, which is cell impermeant, selectively detected exocytosed GLUT4. Using this probe, we verified the 'log' of the trafficking, in which N-glycan-deficient GLUT4 was transiently translocated to the cell membrane upon insulin stimulation and was rapidly internalized without retention on the cell membrane. The results strongly suggest that the N-glycan functions in the retention of GLUT4 on the cell membrane. This study showed the utility of the fluorogenic probes and indicated that this imaging tool will be applicable for research on various membrane proteins that show dynamic changes in localization.
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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.