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Damaged mitochondria can be degraded through a type of organelle-specific autophagy called mitophagy. The Ser/ Thr kinase PTEN-induced putative kinase 1 (PINK1) and the ubiquitin E3 ligase Parkin (Parkinson juvenile disease protein 2, PARK2) are known to promote mitophagy. Parkin ubiquitylates mitochondrial proteins and causes mitochondria to become engulfed by isolation membranes that then fuse with lysosomes (figure bellow). In this model, the autophagy adaptor protein p62/ SQSTM1 (p62) binds to ubiquitinated proteins via its ubiquitinassociated domain and to LC3 on the phagophore via its LC3- interacting region. Thus, the binding of p62 to ubiquitinated mitochondrial proteins tethers the mitochondrion to the LC3- positive phagophore for engulfment. PARKIN also interacts with AMBRA1 (Activating molecule in Beclin-1-regulated autophagy protein 1) at mitochondria to promote mitochondrial clearance, and depolarization of mitochondria increases the interaction between Parkin and AMBRA1.

Fluorescent confocal image of NCI-H460 cells stained with Parkin Antibody (N-term)(Cat#AP6402a). NCI-H460 cells were fixed with 4% PFA (20 min), permeabilized with Triton X-100 (0.2%, 30 min) and incubated with Parkin primary antibody. For secondary antibody, Alexa Fluor® 488 conjugated donkey anti-rabbit antibody (green) was used (1:1000, 1h). Actin filaments have been labeled with Alexa Fluor 555 phalloidin (red).Nuclei were counterstained with DAPI.

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