Publications by authors named "Chris Padovani"
Eukaryotic cells possess hundreds of protein complexes that contain multiple subunits and must be formed at the correct time and place during development. Despite specific assembly pathways, cells frequently encounter complexes with missing or aberrant subunits that can disrupt important signaling events. Cells, therefore, employ several ubiquitin-dependent quality control pathways that can prevent, correct, or degrade flawed complexes.
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- Protein-protein interactions (PPIs) between E3 ubiquitin ligases and substrates are essential for cellular functions, and small molecules that enhance these interactions have potential therapeutic uses.
- Researchers have designed potent small molecules that boost the interaction between the oncogenic transcription factor β-Catenin and its E3 ligase SCF, which in turn promotes the degradation of mutant β-Catenin.
- This new 'molecular glue' approach diverges from traditional PROTACs by directly targeting the interaction interface of PPIs, holding promise for the development of drugs targeting challenging proteins.
Polyubiquitin chains target protein substrates to the 26S proteasome, where they are removed by the deubiquitinase Rpn11 to allow efficient substrate degradation. Despite Rpn11's essential function during substrate processing, its detailed structural and biochemical characterization has been hindered by difficulties in purifying the isolated enzyme. Here we report the 2.
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