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.
中科院分区:
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.
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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影响因子:
64.5
作者:
Katzmann, DJ;Babst, M;Emr, SD
通讯作者:
Emr, SD
DOI:
10.1093/bioinformatics/btq235
发表时间:
2010-06-15
期刊:
Bioinformatics (Oxford, England)
影响因子:
--
作者:
de Souza RF;Aravind L
通讯作者:
Aravind L
影响因子:
5.4
作者:
Mansouri, Mandana;Viswanathan, Kasinath;Frueh, Klaus
通讯作者:
Frueh, Klaus
影响因子:
12.4
作者:
Hurley JH;Stenmark H
通讯作者:
Stenmark H
影响因子:
30.3
作者:
Goffinet, Christine;Allespach, Ina;Keppler, Oliver T.
通讯作者:
Keppler, Oliver T.