Actin cytoskeletal dynamics in T lymphocyte activation and migration
Dynamic rearrangements of the actin cytoskeleton are crucial for the function of numerous cellular elements including T lymphocytes. They are required for migration of T lymphocytes through the body to scan for the presence of antigens, as well as for the formation and stabilization of the immunolog...
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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
01 January 2003
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| In: |
Journal of leukocyte biology
Year: 2003, Volume: 73, Issue: 1, Pages: 30-48 |
| ISSN: | 1938-3673 |
| DOI: | 10.1189/jlb.0602272 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1189/jlb.0602272 Verlag, lizenzpflichtig, Volltext: https://jlb.onlinelibrary.wiley.com/doi/full/10.1189/jlb.0602272 
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| Author Notes: | Yvonne Samstag, Sybille M. Eibert, Martin Klemke, Guido H. Wabnitz |
| Summary: | Dynamic rearrangements of the actin cytoskeleton are crucial for the function of numerous cellular elements including T lymphocytes. They are required for migration of T lymphocytes through the body to scan for the presence of antigens, as well as for the formation and stabilization of the immunological synapse at the interface between antigen-presenting cells and T lymphocytes. Supramolecular activation clusters within the immunological synapse play an important role for the initiation of T cell responses and for the execution of T cell effector functions. In addition to the T cell receptor/CD3 induced actin nucleation via Wasp/Arp2/3-activation, signals through accessory receptors of the T cell (i.e., costimulation) regulate actin cytoskeletal dynamics. In this regard, the actin-binding proteins cofilin and L-plastin represent prominent candidates linking accessory receptor stimulation to the rearrangement of the actin cytoskeleton. Cofilin enhances actin polymerization via its actin-severing activity, and as a long-lasting effect, cofilin generates novel actin monomers through F-actin depolymerization. L-plastin stabilizes actin filament structures by means of its actin-bundling activity. |
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| Item Description: | Gesehen am 22.02.2021 |
| Physical Description: | Online Resource |
| ISSN: | 1938-3673 |
| DOI: | 10.1189/jlb.0602272 |