The UBAP1 Subunit of ESCRT-I Interacts with Ubiquitin via a SOUBA Domain

被引：88

作者：

Agromayor, Monica ^{[1
]}

Soler, Nicolas ^{[2
]}

Caballe, Anna ^{[1
]}

Kueck, Tonya ^{[1
]}

Freund, Stefan M. ^{[2
]}

Allen, Mark D. ^{[2
]}

Bycroft, Mark ^{[2
]}

Perisic, Olga ^{[2
]}

Ye, Yu ^{[2
]}

McDonald, Bethan ^{[1
]}

Scheel, Hartmut ^{[3
]}

Hofmann, Kay ^{[3
]}

Neil, Stuart J. D. ^{[1
]}

Martin-Serrano, Juan ^{[1
]}

Williams, Roger L. ^{[2
]}

机构：

[1] Kings Coll London, Sch Med, Dept Infect Dis, London SE1 9RT, England

[2] MRC, Mol Biol Lab, Cambridge CB2 0QH, England

[3] Miltenyi Biotec, D-51429 Bergisch Gladbach, Germany

来源：

STRUCTURE | 2012年 / 20卷 / 03期

基金：

英国惠康基金; 英国医学研究理事会;

关键词：

LYS48-LINKED POLYUBIQUITIN CHAIN; SORTING COMPLEX; RESTRICTION FACTOR; BINDING DOMAINS; DOWN-REGULATION; PROTEIN; CYTOKINESIS; RECOGNITION; COMPONENT; MECHANISM;

D O I：

10.1016/j.str.2011.12.013

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：414 / 428

页数：15

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