The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA domain.

The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA domain.
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DOI:
10.1016/j.str.2011.12.013
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发表时间:
2012-03-07
期刊:
影响因子:
5.7
通讯作者:
Williams, Roger L.
Williams, Roger L.
中科院分区:
生物学2区
文献类型:
--
作者:
Agromayor, Monica;Soler, Nicolas;Caballe, Anna;Kueck, Tonya;Freund, Stefan M.;Allen, Mark D.;Bycroft, Mark;Perisic, Olga;Ye, Yu;McDonald, Bethan;Scheel, Hartmut;Hofmann, Kay;Neil, Stuart J. D.;Martin-Serrano, Juan;Williams, Roger L.

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转运所需的内体分选复合物(ESCRT)促进泛素化货物的内体分选、MVB生物发生、胞质分裂的晚期和逆转录病毒出芽。在这里,我们表明,泛素相关蛋白1(UBAP 1),一个亚基的人ESCRT-1,coassemble在一个稳定的1:1:1:1复合物与VPS 23/TSG 101,VPS 28,和VPS 37。UBAP 1的C-末端区域的X-射线晶体结构揭示了一个域,我们将其描述为重叠UBA(SOUBA)的螺线管。核磁共振分析表明,每三个刚性排列的重叠UBA组成的SOUBA与泛素相互作用。我们证明,UBAP 1含有ESCRT-I是必不可少的降解抗病毒细胞表面蛋白,如拴系蛋白(BST-2/CD 317),通过病毒对策,即HIV-1辅助蛋白Vpu和卡波西肉瘤相关疱疹病毒(KSHV)泛素连接酶K5。UBAP 1亚基UBAP 1是降解抗病毒蛋白质系链蛋白所必需的。UBAP 1具有由重叠UBA螺线管(SOUBA)组成的结构域。SOUBA中的三个UBA中的每一个都结合单泛素。
The endosomal sorting complexes required for transport (ESCRTs) facilitate endosomal sorting of ubiquitinated cargo, MVB biogenesis, late stages of cytokinesis, and retroviral budding. Here we show that ubiquitin associated protein 1 (UBAP1), a subunit of human ESCRT-I, coassembles in a stable 1:1:1:1 complex with Vps23/TSG101, VPS28, and VPS37. The X-ray crystal structure of the C-terminal region of UBAP1 reveals a domain that we describe as a solenoid of overlapping UBAs (SOUBA). NMR analysis shows that each of the three rigidly arranged overlapping UBAs making up the SOUBA interact with ubiquitin. We demonstrate that UBAP1-containing ESCRT-I is essential for degradation of antiviral cell-surface proteins, such as tetherin (BST-2/CD317), by viral countermeasures, namely, the HIV-1 accessory protein Vpu and the Kaposi sarcoma-associated herpesvirus (KSHV) ubiquitin ligase K5. ► ESCRT-I subunit UBAP1 is essential for degradation of antiviral protein tetherin ► UBAP1 has a domain consisting of a solenoid of overlapping UBAs (SOUBA) ► Each of the three UBAs in the SOUBA binds monoubiquitin
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