PXD047229 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Noncanonical assembly, neddylation, and chimeric cullin-RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex |
Description | Ubiquitin ligation is typically executed by hallmark E3 catalytic domains. Two such domains, "cullin-RING" and "RBR", are individually found in several hundred E3 ligases in humans, and collaborate with E2 enzymes to catalyze ubiquitylation. However, the vertebrate-specific CUL9 complex with RBX1 (also called ROC1), of interest due to its tumor suppressive interaction with TP53, uniquely encompasses both cullin-RING and RBR domains. Here, cryo-EM, biochemistry, and cellular assays elucidate a 1.8 MDa hexameric CUL9-RBX1 assembly. Within one dimeric subcomplex, an E2-bound RBR domain is activated by neddylation of its own cullin domain and positioning from the adjacent CUL9-RBX1 in trans. Our data show CUL9 as unique amongst RBX1-bound cullins in dependence on the metazoan-specific UBE2F neddylation enzyme, while the RBR domain protects it from deneddylation. Substrate ubiquitylation relies on both CUL9's neddylated cullin and RBR domains achieving self-assembled and chimeric cullin-RING/RBR E3 ligase activity. |
HostingRepository | PRIDE |
AnnounceDate | 2024-04-09 |
AnnouncementXML | Submission_2024-04-09_07:43:07.217.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Barbara Steigenberger |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | No PTMs are included in the dataset |
Instrument | Q Exactive HF; Orbitrap Exploris 480 |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2023-11-24 15:28:13 | ID requested | |
⏵ 1 | 2024-04-09 07:43:07 | announced | |
Publication List
Keyword List
submitter keyword: Ubiquitin, RBX1, TP53, APEX2, NEDD8, RBR, cullin, CUL9, E3-ligase |
Contact List
Brenda A. Schulman |
contact affiliation | Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, 82152, Martinsried, Germany |
contact email | schulman@biochem.mpg.de |
lab head | |
Barbara Steigenberger |
contact affiliation | MPI of Biochemistry |
contact email | steigenberger@biochem.mpg.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/04/PXD047229 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD047229
- Label: PRIDE project
- Name: Noncanonical assembly, neddylation, and chimeric cullin-RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex