ATG4C, a member of the ATG4 cysteine protease family, plays a critical role in autophagy, a conserved cellular degradation process essential for maintaining homeostasis. Autophagy involves the formation of double-membrane vesicles (autophagosomes) that engulf cytoplasmic components for lysosomal breakdown. ATG4 proteases, including ATG4A-D, are pivotal in processing and recycling LC3 (microtubule-associated protein 1A/1B-light chain 3), a key protein in autophagosome maturation. Specifically, ATG4C cleaves pro-LC3 to expose its C-terminal glycine, enabling conjugation to phosphatidylethanolamine (PE) on autophagosomal membranes. Later, ATG4C also delipidates LC3-PE to recycle LC3 for subsequent autophagy cycles.
ATG4C antibodies are vital tools for studying autophagy dynamics, enabling researchers to detect ATG4C expression, localization, and interaction partners via techniques like Western blotting, immunofluorescence, and immunoprecipitation. Dysregulation of ATG4C has been linked to diseases such as cancer and neurodegenerative disorders, making these antibodies valuable for exploring pathological mechanisms. While ATG4B is considered the primary LC3-processing enzyme, ATG4C may compensate under stress conditions or in specific tissues, highlighting its context-dependent role.
Research using ATG4C antibodies has advanced understanding of autophagy-related pathways, therapeutic targeting, and disease biomarkers. However, antibody specificity remains a consideration due to homology among ATG4 family members. Validated antibodies are crucial for distinguishing ATG4C from paralogs in experimental models.