Rap1 and Integrin Inside-Out Signaling
Rap1 and Integrin Inside-Out Signaling
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DOI：
10.1007/978-1-61779-166-6_18
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发表时间：
2011-01-01
期刊：
影响因子：
--
通讯作者：
Kinashi, Tatsuo
中科院分区：
文献类型：
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作者：
Katagiri, Koko;Kinashi, Tatsuo
在白细胞中，整合素在与内皮细胞、抗原呈递细胞的粘附相互作用和效应子功能如细胞毒性中发挥重要作用。本章介绍了研究Ras邻近1（Rap 1）的方法，Rap 1是一种信号分子，已越来越多地被认为是免疫系统中整合素介导的细胞粘附以及止血的重要调节因子。Rap 1被多种外部刺激激活，包括趋化因子和抗原。经由Rap 1的信号传导将由内而外的信号传递到整联蛋白，从而增加对配体如免疫球蛋白超家族蛋白以及细胞外基质蛋白和血浆蛋白的亲和力。该过程诱导白细胞粘附到内皮细胞和抗原呈递细胞。除了整联蛋白调节，激活Rap 1诱导淋巴细胞的细胞极性，这与LFA-1重新分布到前沿相协调。
In leukocytes, integrins play important roles in adhesive interactions with endothelium, antigen-presenting cells, and effector functions such as cytotoxicity. This chapter describes methods to study Ras proximity 1 (Rap 1), a signaling molecule that has been increasingly recognized as an important regulator of integrin-mediated cell adhesion in the immune system as well as hemostasis. Rap1 is activated by a wide variety of external stimuli including chemokines and antigens. Signaling via Rap1 transmits an inside-out signal to the integrins, thereby increasing adhesiveness to ligands such as immunoglobulin superfamily proteins as well as extracellular matrix proteins and plasma proteins. This process induces leukocyte cell adhesion to the endothelium and antigen-presenting cells. In addition to integrin regulation, activated Rap1 induces cell polarity of lymphocytes, which is coordinated with LFA-1 redistribution to the leading edge.