The ubiquitin system is governed by the transient assembly of conformationally dynamic complexes. We are fascinated by how these molecular machines form and function in response to stimuli ranging from endogenous signals to degrader drugs mediating targeted protein degradation. We employ an integrated multidisciplinary approach to investigate crosstalk between cellular perturbations and the ubiquitin system—ranging from the development of chemical biology probes and proteomic profiling techniques, to in situ visualization of assemblies using cryo-electron tomography. We then aim to reconstitute these systems to uncover the underlying biochemical and high-resolution structural mechanisms. In this talk, I will present our latest findings on the visualization of dynamic assemblies involved in ubiquitin-mediated regulation.