Academy/Targeted Protein Degradation

Targeted Protein Degradation

Beyond PROTACs: the expanding universe of induced proximity degradation. From ubiquitin-proteasome hijacking to lysosomal targeting and RNA cleavage, TPD modalities are redefining what it means to drug a target.

TPD Modality Comparison

ModalityMechanismTarget LocationE3 LigaseDegradation Pathway
PROTACsBifunctional linker recruits E3 ligase to targetIntracellularVHL, CRBN, IAPsUbiquitin-Proteasome (UPS)
Molecular GluesStabilizes neo-substrate interface on E3 ligaseIntracellularCRBN, DCAF15Ubiquitin-Proteasome (UPS)
LYTACsConjugate binds lysosome-targeting receptor + targetExtracellular / MembraneN/AEndo-Lysosomal
AbTACsBispecific antibody bridges membrane E3 + targetCell SurfaceRNF43, ZNRF3Endo-lysosomal (ubiquitin-assisted)
AUTACsS-guanine tag drives K63-polyUb → p62/LC3 captureIntracellular / OrganellesK63-Ub (no single defined E3)Autophagy-Lysosome
ATTECsBifunctional molecule tethers target directly to LC3Intracellular / AggregatesN/A (ubiquitin-independent)Autophagy-Lysosome
RIBOTACsRecruits RNase L to target RNAIntracellular (RNA)N/ARNase L Cleavage

Interactive Tools

Why Kinetics Matter Across All TPD Modalities: Every TPD modality depends on induced proximity, and the duration and stability of that proximity complex shape degradation efficiency. For protein-targeting degraders (PROTACs, glues, LYTACs, AbTACs), SPR and BLI are the workhorses; RNA-targeting RIBOTACs and receptor-engagement assays for LYTACs/AbTACs typically rely on fluorescence anisotropy and cellular readouts in addition to label-free methods.