Our paper on biophysical investigation of interactions and assembly of full-size SOCS2:EloBC:Cul5:Rbx2 E3 ubiquitin ligase is now published in J. Biol. Chem.

  • Just In Press in JBC
  • Fig. 1. Components of CRL5SOCS2 E3 ligase can be captured from cell lysate using phosphorylated substrate peptide attached to the beads.
  • Fig. 2. ITC data demonstrates weak interaction of SOCS2-EloBC with phosphorylated substrate GHR and tight interaction with scaffold Cul5NTD.
  • Fig. 3. Recombinant components of CRL5SOCS2 assemble into the monomeric full-size protein complex.
  • Fig. 4. Ion mobility drift-time plot (top), corresponding native mass spectra (middle) and collision cross sections (bottom) are shown for the CRL5SOCS2 complexes and their components.
  • Fig. 5. Experimental ion mobility data for a range of charge states suggests an increase in CCS values upon neddylation of the protein complexes.
  • Fig. 6. Gel filtration UV traces.
  • Fig. 7. Native MS spectra.
  • Fig. 8. SDS-PAGE gel images of the neddylation reaction products.
  • Fig. 9. Comparison of Native MS spectra.
  • Fig. 10. Structural models provide important insights into the assembly and architecture of CRL5SOCS2.

Read our Just In Press article here.