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TitleCUL5-ARIH2 E3-E3 ubiquitin ligase structure reveals cullin-specific NEDD8 activation.
Journal, issue, pagesNat Chem Biol, Vol. 17, Issue 10, Page 1075-1083, Year 2021
Publish dateSep 13, 2021
AuthorsSebastian Kostrhon / J Rajan Prabu / Kheewoong Baek / Daniel Horn-Ghetko / Susanne von Gronau / Maren Klügel / Jérôme Basquin / Arno F Alpi / Brenda A Schulman /
PubMed AbstractAn emerging mechanism of ubiquitylation involves partnering of two distinct E3 ligases. In the best-characterized E3-E3 pathways, ARIH-family RING-between-RING (RBR) E3s ligate ubiquitin to ...An emerging mechanism of ubiquitylation involves partnering of two distinct E3 ligases. In the best-characterized E3-E3 pathways, ARIH-family RING-between-RING (RBR) E3s ligate ubiquitin to substrates of neddylated cullin-RING E3s. The E3 ARIH2 has been implicated in ubiquitylation of substrates of neddylated CUL5-RBX2-based E3s, including APOBEC3-family substrates of the host E3 hijacked by HIV-1 virion infectivity factor (Vif). However, the structural mechanisms remained elusive. Here structural and biochemical analyses reveal distinctive ARIH2 autoinhibition, and activation on assembly with neddylated CUL5-RBX2. Comparison to structures of E3-E3 assemblies comprising ARIH1 and neddylated CUL1-RBX1-based E3s shows cullin-specific regulation by NEDD8. Whereas CUL1-linked NEDD8 directly recruits ARIH1, CUL5-linked NEDD8 does not bind ARIH2. Instead, the data reveal an allosteric mechanism. NEDD8 uniquely contacts covalently linked CUL5, and elicits structural rearrangements that unveil cryptic ARIH2-binding sites. The data reveal how a ubiquitin-like protein induces protein-protein interactions indirectly, through allostery. Allosteric specificity of ubiquitin-like protein modifications may offer opportunities for therapeutic targeting.
External linksNat Chem Biol / PubMed:34518685 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.45 - 6.8 Å
Structure data

12995

7oni

EMDB-12995, PDB-7oni:
Structure of Neddylated CUL5 C-terminal region-RBX2-ARIH2*
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-12998:
Structure of Neddylated CRL5Vif-CBFbeta-ARIH2*-APOBEC3C (A3C fullcomplex consensus )
Method: EM (single particle) / Resolution: 6.8 Å

EMDB-12999:
Structure of Neddylated CUL5 C-terminal region-RBX2-ARIH2* ( A3G E3-E3 catalytic focused )
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-13000:
Structure of Neddylated CRL5Vif-CBFbeta-ARIH2*-APOBEC3C (A3C consensus )
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-13001:
Structure of Neddylated CRL5Vif-CBFbeta-ARIH2*-APOBEC3G ( A3G consensus )
Method: EM (single particle) / Resolution: 3.8 Å

PDB-7od1:
Crystal structure of RBR ubiquitin ligase ARIH2
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLIGASE / TRIAD1 / ARIH2 / RBR / Ubiquitin / E3 Ligase / CUL5 / NEDD8 / UBQ / RBX2

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