小柯机器人

英国剑桥大学Andrew P. Carter研究小组发现，微管上的动力蛋白-动力激活蛋白结构显示出串联的适配体结合。该研究于2022年9月7日在线发表于国际一流学术期刊《自然》。

研究人员开发了一个冷冻电镜处理管线，用于解析动力蛋白-动力激活蛋白和适配体BICDR1与微管结合的高分辨率结构。这揭示了相邻的动力蛋白运动域之间的不对称相互作用以及它们与运动行为的关系。研究人员发现，有两个适配体占据了这个复合体。两种适配体与动力蛋白进行类似的相互作用，但在彼此和动力激活蛋白的接触中存在分歧。这些结构对宿主招募马达的稳定性和随机性有影响。

据介绍，细胞质动力蛋白是一种微管马达，由其辅助因子动力激活蛋白和一个卷曲螺旋货物适配体激活。每个动力激活蛋白可以招募多达两个动力蛋白二聚体，它们之间的相互作用影响它们的联合运动行为。不同的适配体与不同的载体相连，有些共享动力蛋白和动力激活蛋白上接触点的模体。关于由此产生的复合体如何与微管相互作用以及适配体如何被招募的结构信息有限。

附：英文原文

Title: Structure of dynein–dynactin on microtubules shows tandem adaptor binding

Author: Chaaban, Sami, Carter, Andrew P.

Issue&Volume: 2022-09-07

Abstract: Cytoplasmic dynein is a microtubule motor that is activated by its cofactor dynactin and a coiled-coil cargo adaptor1,2,3. Up to two dynein dimers can be recruited per dynactin, and interactions between them affect their combined motile behaviour4,5,6. Different coiled-coil adaptors are linked to different cargos7,8, and some share motifs known to contact sites on dynein and dynactin4,9,10,11,12,13. There is limited structural information on how the resulting complex interacts with microtubules and how adaptors are recruited. Here we develop a cryo-electron microscopy processing pipeline to solve the high-resolution structure of dynein–dynactin and the adaptor BICDR1 bound to microtubules. This reveals the asymmetric interactions between neighbouring dynein motor domains and how they relate to motile behaviour. We found that two adaptors occupy the complex. Both adaptors make similar interactions with the dyneins but diverge in their contacts with each other and dynactin. Our structure has implications for the stability and stoichiometry of motor recruitment by cargos.

DOI: 10.1038/s41586-022-05186-y

Source: https://www.nature.com/articles/s41586-022-05186-y

Nature：《自然》，创刊于1869年。隶属于施普林格·自然出版集团，最新IF：69.504
官方网址：http://www.nature.com/
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