LC3GABARAPhoz

LC3GABARAPhoz, also known as LC3-associated endocytosis (LANDO), is a cellular process that plays a role in the degradation of certain extracellular pathogens and intracellular protein aggregates. It is a mechanism distinct from canonical autophagy, though it shares some components with the autophagic machinery. Specifically, LC3GABARAPhoz involves the conjugation of the ubiquitin-like protein LC3 (microtubule-associated protein 1A/1B-light chain 3) and GABARAP (GABA(A) receptor-associated protein) to the membrane of endosomes containing cargo destined for degradation. This conjugation is typically mediated by an E2 ubiquitin-conjugating enzyme and an E3 ubiquitin ligase complex.

The process is initiated by the recognition of specific pathogen-associated molecular patterns or aggregated proteins by pattern recognition receptors on the cell surface, leading to the formation of endosomes. Subsequently, LC3 and GABARAP are recruited and lipidated onto the endosomal membrane, marking it for fusion with lysosomes. This fusion event delivers the cargo to the lysosome for breakdown by hydrolytic enzymes. LC3GABARAPhoz has been implicated in the clearance of bacteria, viruses, and misfolded proteins, contributing to cellular homeostasis and innate immunity. Dysregulation of this pathway has been associated with various diseases, including neurodegenerative disorders and infectious diseases. Further research is ongoing to fully elucidate the molecular mechanisms and physiological significance of LC3GABARAPhoz.