ArticleProceedings of the National Academy of Sciences of the United States of America2012
Plasticity of the asialoglycoprotein receptor deciphered by ensemble FRET imaging and single-molecule counting PALM imaging.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 68 citations in OpenAlex.
- Compositional and topological determinants of a physiological Ashwell-Morell receptor ligand.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Asialoglycoprotein receptor 1: a multifaceted receptor in the liver and cardiovascular system.Frontiers in medicine · 2025Review
- Targeted delivery of oligonucleotides using multivalent protein-carbohydrate interactions.Chemical Society reviews · 2023Review
- Quantifying molecular- to cellular-level forces in living cells.Journal of physics D: Applied physics · 2021Article
- The evolution of a cell biologist.Molecular biology of the cell · 2020Article
- Dissecting Oligomeric States with Photoactivated Localization Microscopy: A Numerical Model.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2020Article
- Bacterial cell growth is arrested by violet and blue, but not yellow light excitation during fluorescence microscopy.BMC molecular and cell biology · 2020Article
- Chromatin nanoscale compaction in live cells visualized by acceptor-to-donor ratio corrected Förster resonance energy transfer between DNA dyes.Journal of biophotonics · 2019Article
- IL-2 receptors preassemble and signal in the ER/Golgi causing resistance to antiproliferative anti-IL-2Rα therapies.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Delivery of GalNAc-Conjugated Splice-Switching ASOs to Non-hepatic Cells through Ectopic Expression of Asialoglycoprotein Receptor.Molecular therapy. Nucleic acids · 2019Article
- Visualizing and discovering cellular structures with super-resolution microscopy.Science (New York, N.Y.) · 2018Review
- Evaluation of GalNAc-siRNA Conjugate Activity in Pre-clinical Animal Models with Reduced Asialoglycoprotein Receptor Expression.Molecular therapy : the journal of the American Society of Gene Therapy · 2018Article
- Advances in Nano Neuroscience: From Nanomaterials to Nanotools.Frontiers in neuroscience · 2018Review
- Counting numbers of synaptic proteins: absolute quantification and single molecule imaging techniques.Neurophotonics · 2016Review
- In Situ Characterization of Bak Clusters Responsible for Cell Death Using Single Molecule Localization Microscopy.Scientific reports · 2016Article
- Quantitative super-resolution imaging with qPAINT.Nature methods · 2016Article
- Galactose as Broad Ligand for Multiple Tumor Imaging and Therapy.Journal of Cancer · 2015Article
- Quantitative analysis of single-molecule superresolution images.Current opinion in structural biology · 2014Review
- Progress in quantitative single-molecule localization microscopy.Histochemistry and cell biology · 2014Review
- Superresolution imaging of biological systems using photoactivated localization microscopy.Chemical reviews · 2014Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The stoichiometry and composition of membrane protein receptors are critical to their function. However, the inability to assess receptor subunit stoichiometry in situ has hampered efforts to relate receptor structures to functional states. Here, we address this problem for the asialoglycoprotein receptor using ensemble FRET imaging, analytical modeling, and single-molecule counting with photoactivated localization microscopy (PALM). We show that the two subunits of asialoglycoprotein receptor [rat hepatic lectin 1 (RHL1) and RHL2] can assemble into both homo- and hetero-oligomeric complexes, displaying three forms with distinct ligand specificities that coexist on the plasma membrane: higher-order homo-oligomers of RHL1, higher-order hetero-oligomers of RHL1 and RHL2 with two-to-one stoichiometry, and the homo-dimer RHL2 with little tendency to further homo-oligomerize. Levels of these complexes can be modulated in the plasma membrane by exogenous ligands. Thus, even a simple two-subunit receptor can exhibit remarkable plasticity in structure, and consequently function, underscoring the importance of deciphering oligomerization in single cells at the single-molecule level.
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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.