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Molecular architecture of the ankyrin SOCS box family of Cul5-dependent E3 ubiquitin ligases.

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Muniz JR, Guo K, Kershaw NJ, Ayinampudi V, von Delft F, Babon JJ, Bullock AN
OpenAccess logo J Mol Biol 425 3166-77 (2013)
Cited: 28 times
EuropePMC logo PMID: 23806657

Abstract

Multi-subunit Cullin-RING E3 ligases often use repeat domain proteins as substrate-specific adaptors. Structures of these macromolecular assemblies are determined for the F-box-containing leucine-rich repeat and WD40 repeat families, but not for the suppressor of cytokine signaling (SOCS)-box-containing ankyrin repeat proteins (ASB1-18), which assemble with Elongins B and C and Cul5. We determined the crystal structures of the ternary complex of ASB9-Elongin B/C as well as the interacting N-terminal domain of Cul5 and used structural comparisons to establish a model for the complete Cul5-based E3 ligase. The structures reveal a distinct architecture of the ASB9 complex that positions the ankyrin domain coaxial to the SOCS box-Elongin B/C complex and perpendicular to other repeat protein complexes. This alternative architecture appears favorable to present the ankyrin domain substrate-binding site to the E2-ubiquitin, while also providing spacing suitable for bulky ASB9 substrates, such as the creatine kinases. The presented Cul5 structure also differs from previous models and deviates from other Cullins via a rigid-body rotation between Cullin repeats. This work highlights the adaptability of repeat domain proteins as scaffolds in substrate recognition and lays the foundation for future structure-function studies of this important E3 family.

Articles - 2wzk mentioned but not cited (8)

  1. Structural basis of PROTAC cooperative recognition for selective protein degradation. Gadd MS, Testa A, Lucas X, Chan KH, Chen W, Lamont DJ, Zengerle M, Ciulli A. Nat Chem Biol 13 514-521 (2017)
  2. Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases. Canning P, Cooper CDO, Krojer T, Murray JW, Pike ACW, Chaikuad A, Keates T, Thangaratnarajah C, Hojzan V, Marsden BD, Gileadi O, Knapp S, von Delft F, Bullock AN. J Biol Chem 288 7803-7814 (2013)
  3. Insights into Cullin-RING E3 ubiquitin ligase recruitment: structure of the VHL-EloBC-Cul2 complex. Nguyen HC, Yang H, Fribourgh JL, Wolfe LS, Xiong Y. Structure 23 441-449 (2015)
  4. Flexible cullins in cullin-RING E3 ligases allosterically regulate ubiquitination. Liu J, Nussinov R. J Biol Chem 286 40934-40942 (2011)
  5. Molecular architecture of the ankyrin SOCS box family of Cul5-dependent E3 ubiquitin ligases. Muniz JR, Guo K, Kershaw NJ, Ayinampudi V, von Delft F, Babon JJ, Bullock AN. J Mol Biol 425 3166-3177 (2013)
  6. Multimeric complexes among ankyrin-repeat and SOCS-box protein 9 (ASB9), ElonginBC, and Cullin 5: insights into the structure and assembly of ECS-type Cullin-RING E3 ubiquitin ligases. Thomas JC, Matak-Vinkovic D, Van Molle I, Ciulli A. Biochemistry 52 5236-5246 (2013)
  7. Structural basis for HIV-1 antagonism of host APOBEC3G via Cullin E3 ligase. Ito F, Alvarez-Cabrera AL, Liu S, Yang H, Shiriaeva A, Zhou ZH, Chen XS. Sci Adv 9 eade3168 (2023)
  8. High Accuracy Prediction of PROTAC Complex Structures. Ignatov M, Jindal A, Kotelnikov S, Beglov D, Posternak G, Tang X, Maisonneuve P, Poda G, Batey RA, Sicheri F, Whitty A, Tonge PJ, Vajda S, Kozakov D. J Am Chem Soc 145 7123-7135 (2023)


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  2. Targeting Cullin-RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation. Bulatov E, Ciulli A. Biochem J 467 365-386 (2015)
  3. Inhibition of IL-6 family cytokines by SOCS3. Babon JJ, Varghese LN, Nicola NA. Semin Immunol 26 13-19 (2014)
  4. The role of cullin 5-containing ubiquitin ligases. Okumura F, Joo-Okumura A, Nakatsukasa K, Kamura T. Cell Div 11 1 (2016)
  5. Poxviral ankyrin proteins. Herbert MH, Squire CJ, Mercer AA. Viruses 7 709-738 (2015)
  6. Cullin-RING E3 Ubiquitin Ligases: Bridges to Destruction. Nguyen HC, Wang W, Xiong Y. Subcell Biochem 83 323-347 (2017)
  7. Chromatin-Bound Cullin-Ring Ligases: Regulatory Roles in DNA Replication and Potential Targeting for Cancer Therapy. Jang SM, Redon CE, Aladjem MI. Front Mol Biosci 5 19 (2018)

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