General Information

ATG4B functions as a cysteine protease with dual activities: proteolytic activity at the C-terminus of ATG8, exposing the C-terminal glycine, and deconjugating or delipidating activity necessary for ATG8 deconjugation (PMID: 11038174). The exposure of glycine at the C-terminus is crucial for conjugating ATG8 proteins to phosphatidylethanolamine (PE) and their insertion into membranes. The crystal structure of HsAtg4B shows a classical papain-like fold addition and a small α/β-fold domain (PMID: 16183633). ATG4B exhibits a preference for GABARAP, GABARAPL1, and LC3 proteins (PMID: 15169837). The knockout or inactivation of ATG4B has been demonstrated to arrest autophagy in cells (PMID: 18768752).

Sequence 3D-Structure Experimental Structures

Monomer

Hetero-Oligomer

Peptide Bound

AlphaFold Structures