Cryo-em structures of gid12-bound gid e3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation

HIGHLIGHTS

• who: Shuai Qiao from the Max Planck Institute University School of Public Health, Boston, MA, USA have published the research: Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation, in the Journal: NATURE COMMUNICATIONS NATURE COMMUNICATIONS
• what: The authors show that both in_vivo and in_vitro Gid12 binds directly to the GID E3 ligase assemblies harboring the substrate receptor Gid4 (Fig1; Supplementary Fig 1b). The authors propose that the nuanced effects of Gid12 on GID E3 ligase activities portend intricate regulation of the diverse multiprotein GID E3 assemblies . . .
  

   

  

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