The prototypic and ubiquitous microtubule motor, kinesin-1, uses a variety of adaptor proteins to facilitate the selective transport of diverse cargo within the cell. These cargo adaptors bind to the motor complex through interactions with the kinesin light or heavy chains (KLCs or KHCs). In this issue of Genes & Development, Dimitrova-Paternoga et al. (pp. 976–991) present the first structural characterization of a KHC–cargo adaptor interface. They describe an antiparallel heterotrimeric coiled-coil complex between the carboxy tail of KHC and Tm1-I/C (aTm1), the atypical tropomyosin that is important for oskar mRNA transport in Drosophila oocytes. This interaction enhances direct binding between KHC and RNA. Their findings demonstrate the structural plasticity of the KHC tail as a platform for protein–protein interactions and reveal how a cargo adaptor protein can modify a motor–RNA interface to promote transport.

中文翻译：

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Kinesin-1 在其适应性线圈中捕获 RNA 货物

原型和普遍存在的微管马达 kinesin-1 使用多种衔接蛋白来促进细胞内多种货物的选择性运输。这些货物适配器通过与驱动蛋白轻链或重链（KLC 或 KHC）的相互作用与运动复合体结合。在本期《基因与发育》中，Dimitrova-Paternoga 等人。(pp. 976–991) 介绍了 KHC-货物适配器接口的第一个结构特征。他们描述了 KHC 的羧基尾和 Tm1-I/C ( a Tm1) 之间的反平行异三聚体卷曲螺旋复合物，这是一种对果蝇中oskar mRNA 转运很重要的非典型原肌球蛋白卵母细胞。这种相互作用增强了 KHC 和 RNA 之间的直接结合。他们的发现证明了 KHC 尾部作为蛋白质-蛋白质相互作用平台的结构可塑性，并揭示了货物衔接蛋白如何修饰马达-RNA 界面以促进运输。