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A novel assay for assessing juxtamembrane and transmembrane domain interactions important for receptor heterodimerization

机译：一种评估对受体异二聚体重要的近膜和跨膜结构域相互作用的新方法

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摘要

Understanding the basis of specificity in receptor homodimerization versus heterodimerization is essential in determining the role receptor plays in signal transduction. Specificity in each of the interfaces formed during signal transduction involves cooperative interactions between receptor extracellular, transmembrane (TM), and cytoplasmic domains. While methods exist for studying receptor heterodimerization in cell membranes, they are limited to either TM domains expressed in an inverted orientation or capture only heterodimerization in a single assay. To address this limitation, we have developed an assay (DN-AraTM) that enables simultaneous measurement of homodimerization and heterodimerization of type I receptor domains in their native orientation, including both soluble and TM domains. Using integrin αIIb and RAGE (receptor for advanced glycation end products) as model type I receptor systems, we demonstrate both specificity and sensitivity of our approach, which will provide a novel tool to identify specific domain interactions that are important in regulating signal transduction.
机译：了解受体同二聚与异二聚的特异性基础对于确定受体在信号转导中的作用至关重要。在信号转导过程中形成的每个界面的特异性都涉及细胞外受体，跨膜（TM）和胞质域之间的协同相互作用。虽然存在研究细胞膜中受体异源二聚化的方法，但它们仅限于以反向定向表达的TM结构域，或仅在一次测定中捕获异源二聚化。为了解决此限制，我们开发了一种测定方法（DN-AraTM），该测定法能够同时测量I型受体域在其天然方向（包括可溶性域和TM域）的均二聚化和异二聚化。使用整联蛋白αIIb和RAGE（晚期糖基化终产物的受体）作为模型I型受体系统，我们展示了我们方法的特异性和敏感性，这将提供一种新颖的工具来鉴定在调节信号转导中重要的特定域相互作用。

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