ArticleBiophysical journal2011
Mechanisms for size-dependent protein segregation at immune synapses assessed with molecular rulers.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
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- Changing the location of proteins on the cell surface is a promising strategy for modulating T cell functions.Immunology · 2024Review
- Antibody agonists trigger immune receptor signaling through local exclusion of receptor-type protein tyrosine phosphatases.Immunity · 2024Article
- Neutralization of the adaptor protein PAG by monoclonal antibody limits murine tumor growth.Molecular therapy. Methods & clinical development · 2022Article
- Trapping or slowing the diffusion of T cell receptors at close contacts initiates T cell signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Costs of Close Contacts: Visualizing the Energy Landscape of Cell Contacts at the Nanoscale.Biophysical journal · 2020Article
- A cell topography-based mechanism for ligand discrimination by the T cell receptor.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- T Cell Microvilli: Sensors or Senders?Frontiers in immunology · 2019Review
- Hydrodynamic trapping measures the interaction between membrane-associated molecules.Scientific reports · 2018Article
- Dimensions and Interactions of Large T-Cell Surface Proteins.Frontiers in immunology · 2018Review
- Visualizing dynamic microvillar search and stabilization during ligand detection by T cells.Science (New York, N.Y.) · 2017Article
- Size-dependent protein segregation at membrane interfaces.Nature physics · 2016Article
- The immune synapse clears and excludes molecules above a size threshold.Nature communications · 2014Article
- Neuroendocrine regulation of inflammation.Seminars in immunology · 2014Review
- A single peptide-major histocompatibility complex ligand triggers digital cytokine secretion in CD4(+) T cells.Immunity · 2013Article
- Article
- Illuminating the dynamics of signal integration in Natural Killer cells.Frontiers in immunology · 2012Article
- New insights into the T cell synapse from single molecule techniques.Nature reviews. Immunology · 2011Review
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Immunological synapses are specialized intercellular contacts formed by several types of immune cells in contact with target cells or antigen-presenting cells. A late-stage immune synapse is commonly a bulls-eye pattern of immune cell receptor-ligand pairs surrounded by integrin complexes. Based on crystal structures, the intermembrane distance would be ∼15 nm for many immune cell receptor-ligand pairs, but ∼40 nm for integrin-ligand pairs. Close proximity of these two classes of intermembrane bonds would require significant membrane bending and such proteins can segregate according to their size, which may be key for receptor triggering. However, tools available to evaluate the intermembrane organization of the synapse are limited. Here, we present what we believe to be a novel approach to test the importance of size in the intercellular organization of proteins, using live-cell microscopy of a size-series of fluorescently-labeled molecules and quantum dots to act as molecular rulers. Small particles readily colocalized at the synapse with MHC class I bound to its cognate natural killer cell receptor, whereas particles larger than 15 nm were increasingly segregated from this interaction. Combined with modeling of the partitioning of the particles by scaled-particle adsorption theory, these molecular rulers show how membrane-bending elasticity can drive size-dependent exclusion of proteins within immune synapses.
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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.