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TitleNoncanonical assembly, neddylation and chimeric cullin-RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex.
Journal, issue, pagesNat Struct Mol Biol, Year 2024
Publish dateApr 11, 2024
AuthorsDaniel Horn-Ghetko / Linus V M Hopf / Ishita Tripathi-Giesgen / Jiale Du / Sebastian Kostrhon / D Tung Vu / Viola Beier / Barbara Steigenberger / J Rajan Prabu / Luca Stier / Elias M Bruss / Matthias Mann / Yue Xiong / Brenda A Schulman /
PubMed AbstractUbiquitin ligation is typically executed by hallmark E3 catalytic domains. Two such domains, 'cullin-RING' and 'RBR', are individually found in several hundred human E3 ligases, and collaborate with ...Ubiquitin ligation is typically executed by hallmark E3 catalytic domains. Two such domains, 'cullin-RING' and 'RBR', are individually found in several hundred human E3 ligases, 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 human 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 among RBX1-bound cullins in dependence on the metazoan-specific UBE2F neddylation enzyme, while the RBR domain protects it from deneddylation. Substrates are recruited to various upstream domains, while ubiquitylation relies on both CUL9's neddylated cullin and RBR domains achieving self-assembled and chimeric cullin-RING/RBR E3 ligase activity.
External linksNat Struct Mol Biol / PubMed:38605244
MethodsEM (single particle)
Resolution3.37 - 13.9 Å
Structure data

18214

8q7e

EMDB-18214, PDB-8q7e:
Structure of CUL9-RBX1 ubiquitin E3 ligase complex - hexameric assembly
Method: EM (single particle) / Resolution: 4.4 Å

18216

8q7h

EMDB-18216, PDB-8q7h:
Structure of CUL9-RBX1 ubiquitin E3 ligase complex in unneddylated and neddylated conformation - focused cullin dimer
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-18217: Structure of CUL9-RBX1 ubiquitin E3 ligase complex in unneddylated and neddylated conformation - focused on E2-like density
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-18218: Structure of CUL9-RBX1 ubiquitin E3 ligase complex in unneddylated and neddylated conformation - focused dimeric core
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-18220: Structure of the hexameric CUL9-RBX1 complex with deletion of CUL9 CPH domain
Method: EM (single particle) / Resolution: 9.5 Å

EMDB-18221: Structure of the hexameric CUL9-RBX1 complex with deletion of CUL9 DOC domain
Method: EM (single particle) / Resolution: 13.7 Å

EMDB-18222: Structure of the hexameric CUL9-RBX1 complex with deletion of CUL9 ARM9 domain
Method: EM (single particle) / Resolution: 12.5 Å

EMDB-18223: Structure of the hexameric CUL9-RBX1 complex with deletion of CUL9 ARIH-RBR element
Method: EM (single particle) / Resolution: 13.9 Å

19179

8rhz

EMDB-19179, PDB-8rhz:
Structure of CUL9-RBX1 ubiquitin E3 ligase complex in unneddylated conformation - symmetry expanded unneddylated dimer
Method: EM (single particle) / Resolution: 3.37 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsLIGASE / Cullin-RING RBR E3 Ligase

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