Specific recruitment of SPA-1 to the immunological synapse: involvement of actin-bundling protein actinin
Specific recruitment of SPA-1 to the immunological synapse: involvement of actin-bundling protein actinin
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DOI：
10.1016/j.imlet.2004.01.004
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发表时间：
2004-04-15
影响因子：
4.4
通讯作者：
Hattori, M
中科院分区：
文献类型：
--
作者：
Harazaki, M;Kawai, Y;Hattori, M
SPA-1通过控制Rap I GT3信号传导参与响应于抗原的T细胞活化的调节。在本研究中，通过使用抗SPA-1抗体和GFP-SPA-1来检查SPA-1在T细胞中的亚细胞定位。SPA-I在漂浮的非极化T细胞表面皮质区弥漫分布，而在肌动蛋白细胞骨架致密的基质粘附区集中分布。在与特异性抗原呈递细胞相互作用后，SPA-1高度集中在与肌动蛋白紧密共定位的免疫突触处。通过酵母双杂交系统，SPA-1与肌动蛋白捆绑蛋白α-辅肌动蛋白相互作用，表明SPA-1与α-辅肌动蛋白共定位于免疫突触。结果表明，T细胞中的SPA-1被选择性地募集到具有密集肌动蛋白-细胞骨架重组的免疫突触中，并持续抑制局部TCR-信号复合物处的Rap1GTP水平以激活T细胞。(C)2004 Elsevier B.V.保留所有权利。
SPA-1 is involved in the regulation of T cell activation in response to antigens through the control of Rap I 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-I 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 alpha-actinin, and it was indicated that SPA-1 co-localized with alpha-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. (C) 2004 Elsevier B.V. All rights reserved.