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The lysosome's hydrolases degrade the autophagosome-delivered contents and its inner membrane. [3] The formation of autophagosomes is regulated by genes that are well-conserved from yeast to higher eukaryotes. The nomenclature of these genes has differed from paper to paper, but it has been simplified in recent years.
Microtubule-associated proteins 1A/1B light chain 3B (hereafter referred to as LC3) is a protein that in humans is encoded by the MAP1LC3B gene. [5] LC3 is a central protein in the autophagy pathway where it functions in autophagy substrate selection and autophagosome biogenesis. LC3 is the most widely used marker of autophagosomes. [6]
ATG may be part of the protein name (such as ATG7) or part of the gene name (such as ATG7), [53] although all ATG proteins and genes do not follow this pattern (such as ULK1). [52] To give specific examples, the UKL1 enzyme (kinase complex) induces autophagosome biogenesis, and ATG13 (Autophagy-related protein 13) is required for phagosome ...
Autophagy-related protein 13 also known as ATG13 is a protein that in humans is encoded by the KIAA0652 gene. [5]ATG13 is an autophagy factor required for phagosome formation. . ATG13 is a target of the TOR kinase signaling pathway that regulates autophagy through phosphorylation of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 comp
Autophagy-related protein 8 (Atg8) is a ubiquitin-like protein required for the formation of autophagosomal membranes. The transient conjugation of Atg8 to the autophagosomal membrane through a ubiquitin -like conjugation system is essential for autophagy in eukaryotes .
The process is tightly regulated and the inflammatory response varies depending on the particle type within the phagosome. Pathogen-infected apoptotic cells will trigger inflammation, but damaged cells that are degraded as part of the normal tissue turnover do not. The response also differs according to the opsonin-mediated phagocytosis.
Conversely, decreased CMA activity associates with increased genome instability and decreased cell survival. CMA is involved in the removal of Chk1, a key protein for cell cycle progression and cells with impaired CMA have defective DNA repair. [26] CMA degrades lipid droplet proteins (perilipin 2 and perilipin 3). [27]
[8] [16] The LRRK2 mutation, G2019S, has also been found to decrease VPS35 levels in mouse N2A neuroblastoma cells, indicating an affective mechanism between these factors. [9] Parkin, an E3 ubiquitin ligase involved in protein degradation, is commonly seen in autosomal recessive juvenile parkinsonism and has known interactions with VPS35. [16]