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Updated: Feb 11, 2026

Visualizing the Actin and Microtubule Cytoskeletons at the B-cell Immune Synapse Using Stimulated Emission Depletion STED Microscopy
Published on: April 9, 2018
Visualizing the Actin and Microtubule Cytoskeletons at the B-cell Immune Synapse Using Stimulated Emission Depletion
Jia C Wang1, Madison Bolger-Munro1, Michael R Gold2
1Department of Microbiology and Immunology, University of British Columbia.
Insights
Researchers developed a super-resolution microscopy method to visualize actin and microtubules in B cells forming an immune synapse. This technique reveals how cytoskeletal dynamics regulate B-cell receptor signaling and activation.
Area of Science:
- Immunology
- Cell Biology
- Microscopy
Background:
- Immune synapse formation in B cells is crucial for B-cell receptor (BCR) signaling and antigen acquisition.
- Cytoskeletal reorganization, involving actin and microtubules, is essential for immune synapse development.
- Understanding the interplay between actin and microtubules, mediated by microtubule-binding proteins, is key to B cell activation.
Purpose of the Study:
- To describe a method using stimulated emission depletion (STED) microscopy for simultaneous imaging of actin, microtubules, and microtubule-binding proteins in B cells.
- To investigate the early events of immune synapse formation and cytoskeletal remodeling.
- To provide insights into how cytoskeletal organization influences B cell activation.
Main Methods:
- Utilized Stimulated Emission Depletion (STED) microscopy for high-resolution imaging.
- Co-imaged actin structures, microtubules, and GFP-tagged microtubule plus-end binding proteins.
- Employed B-lymphoma cells induced to form immune synapses by spreading on anti-immunoglobulin (anti-Ig) coated coverslips.
Main Results:
- Successfully visualized the simultaneous organization of actin, microtubules, and microtubule-binding proteins within the B cell immune synapse.
- High-resolution images revealed detailed cytoskeletal network dynamics during early immune synapse formation.
- Demonstrated the utility of STED microscopy in studying the physical links between actin and microtubule cytoskeletons.
Conclusions:
- The developed STED microscopy protocol enables simultaneous visualization of key cytoskeletal components in B cells.
- This method provides unprecedented detail into the coordinated reorganization of actin and microtubules during immune synapse formation.
- Findings contribute to a deeper understanding of B cell activation mechanisms regulated by cytoskeletal dynamics.
Abstract:
B cells that bind to membrane-bound antigens (e.g., on the surface of an antigen-presenting cell) form an immune synapse, a specialized cellular structure that optimizes B-cell receptor (BCR) signaling and BCR-mediated antigen acquisition. Both the remodeling of the actin cytoskeleton and the reorientation of the microtubule network towards the antigen contact site are essential for immune synapse formation. Remodeling of the actin cytoskeleton into a dense peripheral ring of F-actin is accompanied by polarization of the microtubule-organizing center towards the immune synapse. Microtubule plus-end binding proteins, as well as cortical plus-end capture proteins mediate physical interactions between the actin and microtubule cytoskeletons, which allow them to be reorganized in a coordinated manner. Elucidating the mechanisms that control this cytoskeletal reorganization, as well as understanding how these cytoskeletal structures shape immune synapse formation and BCR signaling, can provide new insights into B cell activation. This has been aided by the development of super-resolution microscopy approaches that reveal new details of cytoskeletal network organization. We describe here a method for using stimulated emission depletion (STED) microscopy to simultaneously image actin structures, microtubules, and transfected GFP-tagged microtubule plus-end binding proteins in B cells. To model the early events in immune synapse formation, we allow B cells to spread on coverslips coated with anti-immunoglobulin (anti-Ig) antibodies, which initiate BCR signaling and cytoskeleton remodeling. We provide step-by-step protocols for expressing GFP fusion proteins in A20 B-lymphoma cells, for anti-Ig-induced cell spreading, and for subsequent cell fixation, Immunostaining, image acquisition, and image deconvolution steps. The high-resolution images obtained using these procedures allow one to simultaneously visualize actin structures, microtubules, and the microtubule plus-end binding proteins that may link these two cytoskeletal networks.
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The Synapse
Emission Spectra
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