Cutting Edge: NK Cell Inhibitory Receptors Prevent Tyrosine Phosphorylation of the Activation Receptor 2B4 (CD244)1
Cutting Edge: NK Cell Inhibitory Receptors Prevent Tyrosine Phosphorylation of the Activation Receptor 2B4 (CD244)1
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最前沿：NK 细胞抑制性受体可防止激活受体 2B4 (CD244)1 的酪氨酸磷酸化
作者：
C. Watzl;C. Stebbins;Eric O Long
2B4是一种NK细胞活化受体，可向其他活化受体提供共刺激信号，其信号转导方式尚不清楚。我们发现2B4在NK细胞上的交联导致其快速酪氨酸磷酸化，这意味着2B4信号传导的初始步骤不需要结合其他受体。在NK细胞-靶细胞相互作用的背景下，2B4的连接导致2B4酪氨酸磷酸化、靶细胞裂解和IFN-γ释放。2B4与杀伤细胞igg样受体（KIR）2DL1或CD94/NKG2的结合完全阻断NK细胞的活化。当KIR2DL1或CD94/NKG2通过其同源MHC I类配体作用于耐药靶细胞时，NK细胞与敏感靶细胞接触时观察到的2B4快速酪氨酸磷酸化被取消。这些结果表明NK抑制受体可以干扰激活受体的磷酸化等近端步骤。
2B4 is an NK cell activation receptor that can provide a costimulatory signal to other activation receptors and whose mode of signal transduction is still unknown. We show that cross-linking of 2B4 on NK cells results in its rapid tyrosine phosphorylation, implying that this initial step in 2B4 signaling does not require coligation of other receptors. Ligation of 2B4 in the context of an NK cell-target cell interaction leads to 2B4 tyrosine phosphorylation, target cell lysis, and IFN-γ release. Coligation of 2B4 with the inhibitory receptors killer cell Ig-like receptor (KIR)2DL1 or CD94/NKG2 completely blocks NK cell activation. The rapid tyrosine phosphorylation of 2B4 observed upon contact of NK cells with sensitive target cells is abrogated when KIR2DL1 or CD94/NKG2 are engaged by their cognate MHC class I ligand on resistant target cells. These results demonstrate that NK inhibitory receptors can interfere with a step as proximal as phosphorylation of an activation receptor.
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影响因子：
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