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Journal article

SPATA2 links CYLD to LUBAC, activates CYLD and controls LUBAC signaling

Abstract:

The Linear UBiquitin chain Assembly Complex (LUBAC) regulates immune signaling and its function is regulated by the deubiquitinases OTULIN and CYLD that associate with the catalytic subunit HOIP. However, the mechanism through which CYLD interacts with HOIP is unclear. We here show that CYLD interacts with HOIP via spermatogenesis-associated protein 2 (SPATA2). SPATA2 interacts with CYLD through its non-canonical PUB domain that binds the catalytic CYLD USP domain in a CYLD B-box-dependent ma...

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Publication status:
Published
Peer review status:
Peer reviewed

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  • (Version of record, pdf, 11.7MB)
Publisher copy:
10.1016/j.molcel.2016.08.001

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Oxford Ludwig Institute
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Oxford Ludwig Institute
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Oxford Ludwig Institute
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Oxford Ludwig Institute
Role:
Author
More from this funder
Name:
Danish Council for Independent Research
Funding agency for:
Gyrd-Hansen, M
Grant:
Sapere Aude Starting Grant
More from this funder
Name:
European Molecular Biology Organization
Funding agency for:
Gyrd-Hansen, M
Grant:
Sapere Aude Starting Grant
More from this funder
Name:
Wellcome Trust
Funding agency for:
Kessler, B
Gyrd-Hansen, M
Grant:
097813/Z/11/Z
Sapere Aude Starting Grant
More from this funder
Name:
John Fell Fund
Funding agency for:
Kessler, B
Grant:
097813/Z/11/Z
More from this funder
Name:
European Research Council
Grant:
309756
Publisher:
Cell Press
Journal:
Molecular Cell More from this journal
Volume:
63
Issue:
6
Pages:
990–1005
Publication date:
2016-08-30
Acceptance date:
2016-07-29
DOI:
ISSN:
1097-4164
Pubs id:
pubs:636510
UUID:
uuid:c9ca6f91-b752-4ff1-a7b2-c00953e3c7cb
Local pid:
pubs:636510
Source identifiers:
636510
Deposit date:
2016-07-29

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