NMR Characterization of Self-Association Domains Promoted by Interactions with LC8 Hub Protein.
NMR Characterization of Self-Association Domains Promoted by Interactions with LC8 Hub Protein.
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DOI：
10.5936/csbj.201402003
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发表时间：
2014
影响因子：
6
通讯作者：
Nyarko A
中科院分区：
文献类型：
--
作者：
Barbar E;Nyarko A
相互作用网络中的大多数蛋白质都有少量的伙伴，而少数被称为枢纽的蛋白质参与大量的相互作用，并在细胞稳态中发挥核心作用。一个高度保守的枢纽是一种叫做LC8的蛋白质，它最初被认为是多亚基复合物动力蛋白的重要组成部分，但后来被证明在不同系统的多种蛋白质复合物中也至关重要。这个中心蛋白的有趣之处在于，它不会被动地结合其各种伙伴，但新出现的证据表明，LC8作为一个二聚化引擎，促进其主要无序的单体伙伴的自我结合和/或更高阶的组织。这种结构组织过程不需要ATP，而是由LC8结合一对形成二价或多价支架的无序链引发的远程变构调节触发。本文综述了LC8在促进其两个结合伙伴（动力蛋白中间链和非动力蛋白Swallow）的自我结合中的作用。
Most proteins in interaction networks have a small number of partners, while a few, called hubs, participate in a large number of interactions and play a central role in cell homeostasis. One highly conserved hub is a protein called LC8 that was originally identified as an essential component of the multi-subunit complex dynein but later shown to be also critical in multiple protein complexes in diverse systems. What is intriguing about this hub protein is that it does not passively bind its various partners but emerging evidence suggests that LC8 acts as a dimerization engine that promotes self-association and/or higher order organization of its primarily disordered monomeric partners. This structural organization process does not require ATP but is triggered by long-range allosteric regulation initiated by LC8 binding a pair of disordered chains forming a bivalent or polybivalent scaffold. This review focuses on the role of LC8 in promoting self-association of two of its binding partners, a dynein intermediate chain and a non dynein protein called Swallow.