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本文引用的文献

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Deciphering the pathway from the TCR to NF-kappaB.解析从T细胞受体到核因子κB的信号通路。
Cell Death Differ. 2006 May;13(5):826-33. doi: 10.1038/sj.cdd.4401856.
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Phosphorylation of CARMA1 plays a critical role in T Cell receptor-mediated NF-kappaB activation.CARMA1的磷酸化在T细胞受体介导的NF-κB激活中起关键作用。
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Phosphorylation of the CARMA1 linker controls NF-kappaB activation.CARMA1连接区的磷酸化调控核因子-κB的激活。
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Constitutive NF-kappaB activation by the t(11;18)(q21;q21) product in MALT lymphoma is linked to deregulated ubiquitin ligase activity.MALT淋巴瘤中t(11;18)(q21;q21)产物导致的组成型核因子κB激活与泛素连接酶活性失调有关。
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PDK1 nucleates T cell receptor-induced signaling complex for NF-kappaB activation.PDK1形成用于激活核因子κB的T细胞受体诱导信号复合物。
Science. 2005 Apr 1;308(5718):114-8. doi: 10.1126/science.1107107.
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Calcium/calmodulin-dependent protein kinase II (CaMKII) localization acts in concert with substrate targeting to create spatial restriction for phosphorylation.钙/钙调蛋白依赖性蛋白激酶II（CaMKII）的定位与底物靶向协同作用，为磷酸化产生空间限制。
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The molecular adapter Carma1 controls entry of IkappaB kinase into the central immune synapse.分子衔接蛋白Carma1控制IκB激酶进入中央免疫突触。
J Exp Med. 2004 Nov 1;200(9):1167-77. doi: 10.1084/jem.20032246.
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The mouse kinome: discovery and comparative genomics of all mouse protein kinases.小鼠激酶组：所有小鼠蛋白激酶的发现与比较基因组学
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Genetic dissection of antigen receptor induced-NF-kappaB activation.抗原受体诱导的核因子κB激活的遗传学剖析
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10
The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes.TRAF6泛素连接酶和TAK1激酶介导T淋巴细胞中BCL10和MALT1对IKK的激活作用。
Mol Cell. 2004 May 7;14(3):289-301. doi: 10.1016/s1097-2765(04)00236-9.

钙离子/钙调蛋白依赖性蛋白激酶II是CARMA1介导的核因子κB激活的调节剂。

Ca2+/calmodulin-dependent protein kinase II is a modulator of CARMA1-mediated NF-kappaB activation.

作者信息

Ishiguro Kazuhiro, Green Todd, Rapley Joseph, Wachtel Heather, Giallourakis Cosmas, Landry Aimee, Cao Zhifang, Lu Naifang, Takafumi Ando, Goto Hidemi, Daly Mark J, Xavier Ramnik J

机构信息

Center for Computational and Integrative Biology, Massachusetts General Hospital, Boston, MA 02114, USA.

出版信息

Mol Cell Biol. 2006 Jul;26(14):5497-508. doi: 10.1128/MCB.02469-05.

DOI:10.1128/MCB.02469-05
PMID:16809782
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1592706/
Abstract

CARMA1 is a central regulator of NF-kappaB activation in lymphocytes. CARMA1 and Bcl10 functionally interact and control NF-kappaB signaling downstream of the T-cell receptor (TCR). Computational analysis of expression neighborhoods of CARMA1-Bcl10MALT 1 for enrichment in kinases identified calmodulin-dependent protein kinase II (CaMKII) as an important component of this pathway. Here we report that Ca(2+)/CaMKII is redistributed to the immune synapse following T-cell activation and that CaMKII is critical for NF-kappaB activation induced by TCR stimulation. Furthermore, CaMKII enhances CARMA1-induced NF-kappaB activation. Moreover, we have shown that CaMKII phosphorylates CARMA1 on Ser109 and that the phosphorylation facilitates the interaction between CARMA1 and Bcl10. These results provide a novel function for CaMKII in TCR signaling and CARMA1-induced NF-kappaB activation.

摘要

CARMA1是淋巴细胞中NF-κB激活的核心调节因子。CARMA1与Bcl10在功能上相互作用，并控制T细胞受体（TCR）下游的NF-κB信号传导。对CARMA1 - Bcl10 - MALT 1表达邻域进行激酶富集的计算分析确定钙调蛋白依赖性蛋白激酶II（CaMKII）是该信号通路的重要组成部分。在此我们报告，T细胞激活后Ca(2+)/CaMKII重新分布至免疫突触，且CaMKII对于TCR刺激诱导的NF-κB激活至关重要。此外，CaMKII增强CARMA1诱导的NF-κB激活。而且，我们已表明CaMKII使CARMA1的Ser109位点磷酸化，该磷酸化促进了CARMA1与Bcl10之间的相互作用。这些结果为CaMKII在TCR信号传导及CARMA1诱导的NF-κB激活中提供了一种新功能。