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Specific recruitment of SPA-1 to the immunological synapse: involvement of actin-bundling protein actinin

Authors
Journal
Immunology Letters
0165-2478
Publisher
Elsevier
Publication Date
Volume
92
Issue
3
Identifiers
DOI: 10.1016/j.imlet.2004.01.004
Keywords
  • Spa-1
  • Rap1
  • Immunological Synapse
  • Actinin
Disciplines
  • Biology
  • Medicine

Abstract

Abstract SPA-1 is involved in the regulation of T cell activation in response to antigens through the control of Rap1 GTPase signaling. In this study, the subcellular localization of SPA-1 in the T cells was examined by using anti-SPA-1 antibody and GFP-SPA-1. While SPA-1 was detected diffusely at the surface cortical region in the floating unpolarized T cells, it was concentrated at the matrix-adhesion region with dense actin-cytoskeleton. Upon interaction with specific antigen-presenting cells, SPA-1 was highly concentrated at the immunological synapse closely co-localizing with actin. By yeast two-hybrid system, SPA-1 was shown to interact with an actin-bundling protein α-actinin, and it was indicated that SPA-1 co-localized with α-actinin at the immunological synapse. The results have suggested that SPA-1 in the T cells is selectively recruited to the immunological synapse with dense actin-cytoskeletal reorganization and keeps restraining the levels of Rap1GTP at the local TCR-signaling complex for the T cell activation.

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