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首页> 外文期刊>Journal of Molecular Biology >Molecular Recognition of M1-Linked Ubiquitin Chains by Native and Phosphorylated UBAN Domains
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Molecular Recognition of M1-Linked Ubiquitin Chains by Native and Phosphorylated UBAN Domains

机译：天然和磷酸化UBAN结构域M1连接的泛素链的分子识别

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摘要

Although the Ub-binding domain in ABIN proteins and NEMO (UBAN) is highly conserved, UBAN-containing proteins exhibit different Ub-binding properties, resulting in their diverse biological roles. Post-translational modifications further control UBAN domain specificity for poly-Ub chains. However, precisely, how the UBAN domain structurally confers such functional diversity remains poorly understood. Here we report crystal structures of ABIN-1 alone and in complex with one or two M1-linked di-Ub chains. ABIN-1 UBAN forms a homo-dimer that provides two symmetrical Ub-binding sites on either side of the coiled-coil structure. Moreover, crystal structures of ABIN1 UBAN in complex with di-Ub chains reveal a concentration-dependency of UBAN/di-Ub binding stoichiometry. Analysis of UBAN/M1-linked di-Ub binding characteristics indicates that phosphorylated S473 in OPTN and its corresponding phospho-mimetic residue in ABIN-1 (E484) are essential for high affinity interactions with M1-linked Ub chains. Also, a phospho-mimetic mutation of A303 in NEMO, corresponding to S473 of OPTN, increases binding affinity for M1-linked Ub chains. These findings are in line with the diverse physiological roles of UBAN domains, as phosphorylation of OPTN UBAN is required to enhance its binding to Ub during mitophagy. (C) 2019 Elsevier Ltd. All rights reserved.
机译：虽然Abin蛋白和NEMO（UBa）中的UB结合结构域高度保守，但含有uban的蛋白质表现出不同的UB结合性质，导致它们不同的生物作用。翻译后修改进一步控制Poly-UB链的uban域特异性。然而，精确地，UBAN领域的结构性地赋予这种功能多样性仍然很差。在这里，我们将Abin-1的晶体结构报告单独和复合物与一个或两个M1连接的DI-UB链条。 Abin-1 uban形成同色二聚体，在卷绕线圈结构的任一侧提供两个对称的UB绑定站点。此外，与DI-UB链复合物中Abin1 uban的晶体结构揭示了uban / di-ub结合化学计量的浓度依赖性。 uban / m1连接的Di-Ub结合特性的分析表明，App-1（E484）中的磷酸化S473及其相应的磷光剂残基是必不可少的与M1连接的UB链的高亲和力相互作用。而且，对应于OPTN的S473的NEMO中A303的磷光剂突变增加了对M1连接的UB链的结合亲和力。这些发现符合uban结构域的不同生理作用，因为optn uban的磷酸化需要在菌道期间增强其对Ub的结合。 （c）2019 Elsevier Ltd.保留所有权利。

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