''Down the rabbit hole: weak protein interactions and biological control''

Most biological responses are underpinned by regulated protein interactions, often mediated by context-dependent recognition of short sequence motifs by modular domains. The dynamics of protein recognition can be exquisitely tuned by complex combinations of weak affinity binding sites, but this malleable recognition code remains largely undeciphered. Case examples of weak interactions that dictate substrate recognition and enzymatic activity in the ubiquitin-proteasome system will be described, including modulation by small molecule probes.