Dynamic release of Cdc34 from SCF. the hand that rocks the cradle.
Polyubiquitylation is a complex but poorly understood biochemical reaction catalyzed by E3 ubiquitin ligases. In this issue of Cell, Deffenbaugh et al. provide experimental support for a model in which the dynamic release of the ubiquitin-charged E2 Cdc34 from its primary binding site within the rigid cradle-like SCF E3 complex allows for unexpected spatial flexibility to assemble a polyubiquitin chain.
D064173:Anaphase-Promoting Complex-Cyclosome; D001665:Binding Sites; D019281:Dimerization; D006801:Humans; D007700:Kinetics; D008025:Ligases / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D019089:Stem Cell Factor / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism*; D044763:Ubiquitin-Conjugating Enzymes; D043743:Ubiquitin-Protein Ligase Complexes
D019089:Stem Cell Factor; D025801:Ubiquitin; C577447:CDC34 protein, human; D044763:Ubiquitin-Conjugating Enzymes; D043743:Ubiquitin-Protein Ligase Complexes; D064173:Anaphase-Promoting Complex-Cyclosome; D008025:Ligases