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Tetrahydrobiopterin modulates ubiquitin conjugation to UBC13/UBE2N and proteasome activity by S-nitrosation

Abstract:

Nitric Oxide (NO) is an intracellular signalling mediator, which affects many biological processes via the posttranslational modification of proteins through S-nitrosation. The availability of NO and NOS-derived reactive oxygen species (ROS) from enzymatic uncoupling are determined by the NO synthase cofactor Tetrahydrobiopterin (BH4). Here, using a global proteomics “biotin-switch” approach, we identified components of the ubiquitin-proteasome system to be altered via BH4-dependent NO signal...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1038/s41598-018-32481-4

Authors


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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
RDM; Cardiovascular Medicine
Oxford college:
Jesus College
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Subgroup:
Target Discovery Institute
Oxford college:
St Anne's College
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
RDM; Cardiovascular Medicine
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
RDM; Cardiovascular Medicine
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Subgroup:
Target Discovery Institute
Role:
Author
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More from this funder
Funding agency for:
Crabtree, MJ
National Institute for Health Research More from this funder
Publisher:
Springer Nature Publisher's website
Journal:
Scientific Reports Journal website
Volume:
8
Pages:
Article: 14310
Publication date:
2018-09-25
Acceptance date:
2018-09-06
DOI:
EISSN:
2045-2322
Pubs id:
pubs:916031
URN:
uri:832d14cb-4529-4e1a-af0e-3e7f0f8a9c33
UUID:
uuid:832d14cb-4529-4e1a-af0e-3e7f0f8a9c33
Local pid:
pubs:916031

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