ArticleBiophysical journal2016
MHC I Expression Regulates Co-clustering and Mobility of Interleukin-2 and -15 Receptors in T Cells.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Mutation of conserved MHC class I cytoplasmic tyrosine affects CD8+ T cell priming, effector function, and memory response.Frontiers in immunology · 2025Article
- Role of C-Terminal Domain and Membrane Potential in the Mobility of Kv1.3 Channels in Immune Synapse Forming T Cells.International journal of molecular sciences · 2022Article
- Homotypic and heterotypicCurrent research in immunology · 2022Review
- IL-15Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- Open MHC Class I Conformers: A Look through the Looking Glass.International journal of molecular sciences · 2021Review
- Thermogenic Activation Downregulates High Mitophagy Rate in Human Masked and Mature Beige Adipocytes.International journal of molecular sciences · 2020Article
- 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
- Minimum degree of overlap between IL-9R and IL-2R on human T lymphoma cells: A quantitative CLSM and FRET analysis.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2018Article
- A Rationale for Mesoscopic Domain Formation in Biomembranes.Biomolecules · 2018Article
- Article
- Membrane Potential Distinctly Modulates Mobility and Signaling of IL-2 and IL-15 Receptors in T Cells.Biophysical journal · 2018Article
- Complexity Revealed: A Hierarchy of Clustered Membrane Proteins.Biophysical journal · 2016Article
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Authors and funding
12 authors at 5 institutions in 4 countries.
Funding
Abstract
MHC glycoproteins form supramolecular clusters with interleukin-2 and -15 receptors in lipid rafts of T cells. The role of highly expressed MHC I in maintaining these clusters is unknown. We knocked down MHC I in FT7.10 human T cells, and studied protein clustering at two hierarchic levels: molecular aggregations and mobility by Förster resonance energy transfer and fluorescence correlation spectroscopy; and segregation into larger domains or superclusters by superresolution stimulated emission depletion microscopy. Fluorescence correlation spectroscopy-based molecular brightness analysis revealed that the studied molecules diffused as tight aggregates of several proteins of a kind. Knockdown reduced the number of MHC I containing molecular aggregates and their average MHC I content, and decreased the heteroassociation of MHC I with IL-2Rα/IL-15Rα. The mobility of not only MHC I but also that of IL-2Rα/IL-15Rα increased, corroborating the general size decrease of tight aggregates. A multifaceted analysis of stimulated emission depletion images revealed that the diameter of MHC I superclusters diminished from 400-600 to 200-300 nm, whereas those of IL-2Rα/IL-15Rα hardly changed. MHC I and IL-2Rα/IL-15Rα colocalized with GM1 ganglioside-rich lipid rafts, but MHC I clusters retracted to smaller subsets of GM1- and IL-2Rα/IL-15Rα-rich areas upon knockdown. Our results prove that changes in expression level may significantly alter the organization and mobility of interacting membrane proteins.
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