Answers are grounded in this paper and cite their sources.
Demonstrates targeted protein degradation in cells, indicating potential for illness treatment.
Targeted protein degradation harnesses endogenous cellular machinery to eliminate disease-causing proteins, yet achieving phenotype-specific degradation across diverse cell types remains challenging. Here we show that antibody-enriched biomolecular condensates formed by liquid–liquid phase separation function as intracellular protein degradation tools, combining cytosolic trafficking with direct proteasome recruitment for targeted substrate clearance. These nanoscale condensates incorporate a short proteasome-targeting motif into phase-separation precursors, preserve antibody activity, enable direct proteasome recruitment, and improve delivery uniformity. When loaded with a mutation-specific antibody, these condensates selectively degrade oncogenic KRAS G12V without affecting wild-type KRAS in heterozygous cells, and suppress tumor growth in a KRAS G12V xenograft model. This strategy provides a modular platform for intracellular protein degradation that can be readily adapted by exchanging antibodies, without requiring genetic modification of cellular system. Targeted protein degradation has huge potential, but phenotype-specific degradation remains a difficulty. Here, a phase-separation biomolecular condensates as an intracellular degradation agent is developed, combining antibody-guided recognition with direct proteasome recruitment to enable phenotype-selective protein clearance.
No takes yet. Share an insight, caveat, or question.
Li et al. (2026) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: