Conformational regulation of AP1 and AP2 clathrin adaptor complexes.,Traffic

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Conformational regulation of AP1 and AP2 clathrin adaptor complexes.
Traffic ( IF 3.6 ) Pub Date : 2019-08-06 , DOI: 10.1111/tra.12677
Gwendolyn M Beacham ₁ , Edward A Partlow ₁ , Gunther Hollopeter ₁

Affiliation

Heterotetrameric clathrin adaptor protein complexes (APs) orchestrate the formation of coated vesicles for transport among organelles of the cell periphery. AP1 binds membranes enriched for phosphatidylinositol 4-phosphate, such as the trans Golgi network, while AP2 associates with phosphatidylinositol 4,5-bisphosphate of the plasma membrane. At their respective membranes, AP1 and AP2 bind the cytoplasmic tails of transmembrane protein cargo and clathrin triskelions, thereby coupling cargo recruitment to coat polymerization. Structural, biochemical and genetic studies have revealed that APs undergo conformational rearrangements and reversible phosphorylation to cycle between different activity states. While membrane, cargo and clathrin have been demonstrated to promote AP activation, growing evidence supports that membrane-associated proteins such as Arf1 and FCHo also stimulate this transition. APs may be returned to the inactive state via a regulated process involving phosphorylation and a protein called NECAP. Finally, because antiviral mechanisms often rely on appropriate trafficking of membrane proteins, viruses have evolved novel strategies to evade host defenses by influencing the conformation of APs. This review will cover recent advances in our understanding of the molecular inputs that stimulate AP1 and AP2 to adopt structurally and functionally distinct configurations.

中文翻译：

AP1和AP2网格蛋白适配器复合物的构象调控。

异四聚体网格蛋白衔接子蛋白复合物（APs）协调包被的囊泡的形成，以在细胞外围的细胞器之间运输。AP1结合富含4-磷酸磷脂酰肌醇的膜，例如反式高尔基网络，而AP2与质膜的磷脂酰肌醇4,5-二磷酸结合。AP1和AP2在它们各自的膜上结合跨膜蛋白货物和网格蛋白triskelions的胞质尾巴，从而使货物募集与外壳聚合反应耦合。结构，生化和遗传研究表明，AP会发生构象重排和可逆磷酸化，从而在不同的活动状态之间循环。虽然膜，货物和网格蛋白已被证明可促进AP活化，越来越多的证据支持与膜相关的蛋白（例如Arf1和FCHo）也能刺激这种转变。通过涉及磷酸化和称为NECAP的蛋白质的调节过程，AP可以恢复为非活性状态。最后，由于抗病毒机制通常依赖于膜蛋白的适当运输，因此病毒已发展出新颖的策略来通过影响AP的构象来逃避宿主防御。这篇综述将涵盖我们对刺激AP1和AP2采取结构上和功能上不同的配置的分子输入的最新进展。由于抗病毒机制通常依赖于膜蛋白的适当运输，因此病毒已发展出新颖的策略来通过影响AP的构象来逃避宿主防御。这篇综述将涵盖我们对刺激AP1和AP2采取结构上和功能上不同的配置的分子输入的最新进展。由于抗病毒机制通常依赖于膜蛋白的适当运输，因此病毒已发展出新颖的策略来通过影响AP的构象来逃避宿主防御。这篇综述将涵盖我们对刺激AP1和AP2采取结构上和功能上不同的配置的分子输入的最新进展。

更新日期：2019-08-06

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