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首页> 外文期刊>Journal of Molecular Biology >Evidence for New Homotypic and Heterotypic Interactions between Transmembrane Helices of Proteins Involved in Receptor Tyrosine Kinase and Neuropilin Signaling
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Evidence for New Homotypic and Heterotypic Interactions between Transmembrane Helices of Proteins Involved in Receptor Tyrosine Kinase and Neuropilin Signaling

机译：受体酪氨酸激酶和神经纤维蛋白信号转导的蛋白质跨膜螺旋之间新的同型和异型相互作用的证据。

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Signaling in eukaryotic cells frequently relies on dynamic interactions of single-pass membrane receptors involving their transmembrane (TM) domains. To search for new such interactions, we have developed a bacterial two-hybrid system to screen for both homotypic and heterotypic interactions between TM helices. We have explored the dimerization of TM domains from 16 proteins involved in both receptor tyrosine kinase and neuropilin signaling. This study has revealed several new interactions. We found that the TM domain of Mucin-4, a putative intramembrane ligand for erbB2, dimerizes not only with erbB2 but also with all four members of the erbB family. In the Neuropilin/Plexin family of receptors, we showed that the TM domains of Neuropilins 1 and 2 dimerize with themselves and also with Plexin-A1, Plexin-B1, and L1 CAM, but we were unable to observe interactions with several other TM domains notably those of members of the VEGF receptor family. The potentially important Neuropilin 1/Plexin-A1 interaction was confirmed using a surface plasmon resonance assay. This work shows that TM domain interactions can be highly specific. Exploring further the propensities of TM helix helix association in cell membrane should have important practical implications related to our understanding of the structure function of bitopic proteins' assembly and subsequent function, especially in the regulation of signal transduction. (C) 2014 Elsevier Ltd. All rights reserved.
机译：真核细胞中的信号传导通常依赖于涉及其跨膜（TM）域的单程膜受体的动态相互作用。为了寻找新的此类相互作用，我们开发了一种细菌双杂交系统来筛选TM螺旋之间的同型和异型相互作用。我们已经从参与受体酪氨酸激酶和神经纤毛蛋白信号传导的16种蛋白质中探索了TM域的二聚化。这项研究揭示了几种新的相互作用。我们发现，Mucin-4的TM结构域是erbB2的假定膜内配体，不仅与erbB2而且与erbB家族的所有四个成员二聚。在Neuropilin / Plexin受体家族中，我们显示了Neuropilins 1和2的TM结构域与它们自身以及Plexin-A1，Plexin-B1和L1 CAM有二聚体，但是我们无法观察到与其他几个TM结构域的相互作用尤其是那些VEGF受体家族的成员。使用表面等离振子共振测定法确认了潜在重要的Neuropilin 1 / Plexin-A1相互作用。这项工作表明TM域交互可以是高度特定的。进一步探索细胞膜中TM螺旋螺旋缔合的倾向，应具有重要的实际意义，这与我们对双位蛋白组装的结构功能和后续功能的理解有关，尤其是在信号转导的调控中。 （C）2014 Elsevier Ltd.保留所有权利。

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