酪氨酸激酶使衔接分子能够对 T 细胞中的趋化因子诱导的 Rap1 激活作出反应。
Tyrosine kinases EnAbling adaptor molecules for chemokine-induced Rap1 activation in T cells.
机构信息
Blood Center of Wisconsin, Blood Research Institute, Milwaukee, WI 53226, USA.
出版信息
Sci Signal. 2012 Jul 31;5(235):pe33. doi: 10.1126/scisignal.2003383.
Abstract
Chemokines regulate T cell trafficking into secondary lymphoid organs and migration across endothelial cells in response to inflammatory signals. The small guanosine triphosphatase Rap1 is a critical regulator of chemokine signaling in T cells, but how chemokines activate Rap1 has been unclear. A study showed that Abl family tyrosine kinases were essential for chemokine-induced Rap1 activation, T cell polarization, and migration. Abl family kinases promoted Rap1 activation by phosphorylating the adaptor protein human enhancer of filamentation 1 (HEF1), thus establishing a critical Abl-HEF1-Rap1 signaling axis for chemokine-induced T cell migration.
摘要
趋化因子调节 T 细胞向次级淋巴器官的迁移，并响应炎症信号穿过内皮细胞。小分子鸟苷三磷酸酶 Rap1 是 T 细胞中趋化因子信号的关键调节剂，但趋化因子如何激活 Rap1 尚不清楚。一项研究表明，Abl 家族酪氨酸激酶对于趋化因子诱导的 Rap1 激活、T 细胞极化和迁移是必需的。Abl 家族激酶通过磷酸化衔接蛋白人伸长因子 1（human enhancer of filamentation 1，HEF1）促进 Rap1 的激活，从而建立了一个关键的 Abl-HEF1-Rap1 信号轴，用于趋化因子诱导的 T 细胞迁移。
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