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

Research output: Contribution to journalArticle

Monica Agromayor, Nicolas Soler, Anna Caballe, Tonya Kueck, Stefan M. Freund, Mark D. Allen, Mark Bycroft, Olga Perisic, Yu Ye, Bethan McDonald, Hartmut Scheel, Kay Hofmann, Stuart J. D. Neil, Juan Martin-Serrano, Roger L. Williams

Original languageEnglish
Pages (from-to)414 - 428
Number of pages15
JournalStructure
Volume20
Issue number3
DOIs
Publication statusPublished - 7 Mar 2012

King's Authors

Abstract

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.

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