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首页> 外文期刊>Cellular Signalling >Kit- and Fc epsilon RI-induced differential phosphorylation of the transmembrane adaptor molecule NTAL/LAB/LAT2 allows flexibility in its scaffolding function in mast cells
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Kit- and Fc epsilon RI-induced differential phosphorylation of the transmembrane adaptor molecule NTAL/LAB/LAT2 allows flexibility in its scaffolding function in mast cells

机译：试剂盒和FcεRI诱导的跨膜衔接分子NTAL / LAB / LAT2的差异磷酸化使肥大细胞的支架功能具有灵活性

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The transmembrane adaptor protein (TRAP), NTAL, is phosphorylated in mast cells following Fc epsilon RI aggregation whereby it cooperates with LAT to induce degranulation. The Kit ligand, stem cell factor (SCF), enhances antigen-induced degranutation and this also appears to be NTAL-dependent. However, Kit and Fc epsilon RI appear to utilize different mechanisms to induce NTAL phosphorylation. Thus, we examined whether the responsible kinases selectively phosphorylated distinct tyrosines in NTAL and explored the implications for downstream signaling. Whereas Fc epsilon RI required Lyn and Syk for NTAL phosphorylation, Kit appeared to directly phosphorylate NTAL. Furthermore, co-transfection studies with NTAL constructs revealed that Lyn, Syk, and Kit phosphorylate different tyrosines in NTAL. The tyrosines principally phosphorylated by Syk were recognized as Grb2-binding sites, whereas Lyn and Kit phosphorylated other tyrosines, both inside and outside of these motifs. Pull down studies revealed that PLC gamma(1) I associated with the two terminal Syk-phosphorylated Grb2-binding sites, which would help to explain the observed decrease in antigen-induced calcium signal and degranulation in NTAL-knock down-human mast cells. The observations reported herein support the conclusion that NTAL may be differentially utilized by specific receptors for relaying alternative signals and this suggests a flexibility in the function of TRAPs not previously appreciated. (C) 2007 Elsevier Inc. All rights reserved.
机译：跨膜衔接蛋白（TRAP）NTAL在FcεRI聚集后在肥大细胞中被磷酸化，从而与LAT协同诱导脱粒。 Kit配体，干细胞因子（SCF），可增强抗原诱导的变性，这也似乎是NTAL依赖性的。但是，Kit和FcεRI似乎利用了不同的机制来诱导NTAL磷酸化。因此，我们检查了负责任的激酶是否在NTAL中选择性磷酸化了不同的酪氨酸，并探讨了其对下游信号传导的影响。 FcεRI要求Lyn和Syk进行NTAL磷酸化，而Kit似乎直接将NTAL磷酸化。此外，与NTAL构建体的共转染研究表明，Lyn，Syk和Kit磷酸化了NTAL中的不同酪氨酸。主要被Syk磷酸化的酪氨酸被认为是Grb2结合位点，而Lyn和Kit磷酸化了这些图案内部和外部的其他酪氨酸。下拉研究表明，PLCγ（1）I与两个末端Syk磷酸化的Grb2结合位点相关，这将有助于解释观察到的抗原诱导的钙信号减少和NTAL敲低人类肥大细胞脱颗粒。本文报道的观察结果支持以下结论：特定受体可以差异地利用NTAL来传递替代信号，这暗示了TRAP功能的灵活性，这一点以前没有得到认识。 （C）2007 Elsevier Inc.保留所有权利。

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