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Demonstration of improvements to the bioluminescence resonance energy transfer (BRET) technology for the monitoring of G protein-coupled receptors in live cells.用于监测活细胞中G蛋白偶联受体的生物发光共振能量转移（BRET）技术改进的演示。
J Biomol Screen. 2008 Oct;13(9):888-98. doi: 10.1177/1087057108324032. Epub 2008 Sep 23.
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How calmodulin interacts with the adenosine A(2A) and the dopamine D(2) receptors.钙调蛋白如何与腺苷A(2A)受体和多巴胺D(2)受体相互作用。
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Detection of heteromerization of more than two proteins by sequential BRET-FRET.通过连续生物发光共振能量转移（BRET）-荧光共振能量转移（FRET）检测两种以上蛋白质的异源二聚化
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An update on adenosine A2A-dopamine D2 receptor interactions: implications for the function of G protein-coupled receptors.腺苷A2A - 多巴胺D2受体相互作用的最新进展：对G蛋白偶联受体功能的影响
Curr Pharm Des. 2008;14(15):1468-74. doi: 10.2174/138161208784480108.
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Mass spectrometric characterization of mitochondrial complex I NDUFA10 variants.线粒体复合物I NDUFA10变体的质谱表征
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Blocking striatal adenosine A2A receptors: a new strategy for basal ganglia disorders.阻断纹状体腺苷A2A受体：治疗基底神经节疾病的新策略。
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Conformational cross-talk between alpha2A-adrenergic and mu-opioid receptors controls cell signaling.α2A-肾上腺素能受体与μ-阿片受体之间的构象串扰控制细胞信号传导。
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Adenosine receptor heteromers and their integrative role in striatal function.腺苷受体异聚体及其在纹状体功能中的整合作用。
ScientificWorldJournal. 2007 Nov 2;7:74-85. doi: 10.1100/tsw.2007.211.
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Evidence that calmodulin binding to the dopamine D2 receptor enhances receptor signaling.钙调蛋白与多巴胺D2受体结合可增强受体信号传导的证据。
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钙调蛋白、腺苷A2A受体与多巴胺D2受体之间的相互作用。

Interactions between calmodulin, adenosine A2A, and dopamine D2 receptors.

作者信息

Navarro Gemma, Aymerich Marisol S, Marcellino Daniel, Cortés Antoni, Casadó Vicent, Mallol Josefa, Canela Enric I, Agnati Luigi, Woods Amina S, Fuxe Kjell, Lluís Carmen, Lanciego Jose Luis, Ferré Sergi, Franco Rafael

机构信息

Institut d'Investigacions Biomèdiques August Pi i Sunyer, Centro de Investigación Biomédica en Red Sobre Enfermedades Neurodegenerativas, and Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Barcelona, 08028 Barcelona, Spain.

Centro de Investigación Médica Aplicada Neurociencias (CIMA), Universidad de Navarra, Avda. Pio XII 55, 31008 Pamplona, Spain.

出版信息

J Biol Chem. 2009 Oct 9;284(41):28058-28068. doi: 10.1074/jbc.M109.034231. Epub 2009 Jul 24.

DOI:10.1074/jbc.M109.034231
PMID:19632986
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2788857/
Abstract

The Ca(2+)-binding protein calmodulin (CaM) has been shown to bind directly to cytoplasmic domains of some G protein-coupled receptors, including the dopamine D(2) receptor. CaM binds to the N-terminal portion of the long third intracellular loop of the D(2) receptor, within an Arg-rich epitope that is also involved in the binding to G(i/o) proteins and to the adenosine A(2A) receptor, with the formation of A(2A)-D(2) receptor heteromers. In the present work, by using proteomics and bioluminescence resonance energy transfer (BRET) techniques, we provide evidence for the binding of CaM to the A(2A) receptor. By using BRET and sequential resonance energy transfer techniques, evidence was obtained for CaM-A(2A)-D(2) receptor oligomerization. BRET competition experiments indicated that, in the A(2A)-D(2) receptor heteromer, CaM binds preferentially to a proximal C terminus epitope of the A(2A) receptor. Furthermore, Ca(2+) was found to induce conformational changes in the CaM-A(2A)-D(2) receptor oligomer and to selectively modulate A(2A) and D(2) receptor-mediated MAPK signaling in the A(2A)-D(2) receptor heteromer. These results may have implications for basal ganglia disorders, since A(2A)-D(2) receptor heteromers are being considered as a target for anti-parkinsonian agents.

摘要

钙结合蛋白钙调蛋白（CaM）已被证明可直接结合某些G蛋白偶联受体的细胞质结构域，包括多巴胺D(2)受体。CaM与D(2)受体长的第三个细胞内环的N端部分结合，位于一个富含精氨酸的表位内，该表位也参与与G(i/o)蛋白和腺苷A(2A)受体的结合，并形成A(2A)-D(2)受体异聚体。在本研究中，通过蛋白质组学和生物发光共振能量转移（BRET）技术，我们提供了CaM与A(2A)受体结合的证据。通过使用BRET和顺序共振能量转移技术，获得了CaM-A(2A)-D(2)受体寡聚化的证据。BRET竞争实验表明，在A(2A)-D(2)受体异聚体中，CaM优先结合到A(2A)受体的近端C端表位。此外，发现Ca(2+)可诱导CaM-A(2A)-D(2)受体寡聚体的构象变化，并选择性调节A(2A)-D(2)受体异聚体中A(2A)和D(2)受体介导的MAPK信号传导。这些结果可能对基底神经节疾病有影响，因为A(2A)-D(2)受体异聚体正被视为抗帕金森病药物的靶点。