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Updated: Aug 8, 2026

Real-time Live Imaging of T-cell Signaling Complex Formation
Published on: June 23, 2013
Cutting edge: integration of human T lymphocyte cytoskeleton by the cytolinker plectin
1Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, 10 Center Drive, Bethesda, MD 20892, USA. BrownM@exchange.nih.gov
Insights
Plectin organizes the lymphocyte cytoskeleton by linking vimentin filaments to other structures. This protein complex is crucial for regulating cell shape changes during immune responses.
Area of Science:
- Cell Biology
- Immunology
- Cytoskeletal Dynamics
Background:
- Lymphocyte polarization is essential for immune cell function.
- Vimentin intermediate filaments (IFs) collapse during polarization, but their interactions are poorly understood.
Purpose of the Study:
- To investigate the role of plectin in lymphocyte cytoskeletal organization.
- To elucidate the interactions of vimentin with other cytoskeletal proteins during T cell polarization.
Main Methods:
- Immunofluorescence microscopy to visualize protein localization in human T lymphocytes.
- Co-immunoprecipitation to identify protein complexes.
- Overexpression studies in Jurkat T cells to assess functional impact.
Main Results:
- Human T lymphocytes express plectin, which binds to vimentin IFs.
- Plectin forms a complex with vimentin, actin, fodrin, moesin, and lamin B.
- During polarization, plectin, vimentin, and fodrin redistribute to the uropod, linking the nucleus to the cell cortex.
- Plectin overexpression causes vimentin aggregation near the nucleus.
Conclusions:
- Plectin is a key organizer of the lymphocyte cytoskeleton.
- The vimentin-plectin-fodrin complex mediates structural integrity during cell polarization.
- Plectin likely regulates lymphocyte cytoarchitecture for processes like extravasation.
Abstract:
Chemokine-induced polarization of lymphocytes involves the rapid collapse of vimentin intermediate filaments (IFs) into an aggregate within the uropod. Little is known about the interactions of lymphocyte vimentin with other cytoskeletal elements. We demonstrate that human peripheral blood T lymphocytes express plectin, an IF-binding, cytoskeletal cross-linking protein. Plectin associates with a complex of structural proteins including vimentin, actin, fodrin, moesin, and lamin B in resting peripheral blood T lymphocytes. During chemokine-induced polarization, plectin redistributes to the uropod associated with vimentin and fodrin; their spatial distribution indicates that this vimentin-plectin-fodrin complex provides a continuous linkage from the nucleus (lamin B) to the cortical cytoskeleton. Overexpression of the plectin IF-binding domain in the T cell line Jurkat induces the perinuclear aggregation of vimentin IFs. Plectin is therefore likely to serve as an important organizer of the lymphocyte cytoskeleton and may regulate changes of lymphocyte cytoarchitecture during polarization and extravasation.
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