Parkin and PINK1 are key proteins involved in mitochondrial quality control and autophagy in Parkinson's disease (PD). PINK1 and Parkin mutations cause autosomal recessive PD. When mitochondrial membrane potential (ΔΨm) is lost, cytosolic Parkin is recruited to mitochondria, promoting mitochondrial autophagy. This study shows that PINK1 is essential for Parkin recruitment to mitochondria. Overexpression of wild-type (WT) PINK1, but not mutated PINK1, causes Parkin translocation to mitochondria even in cells with normal ΔΨm. Once at mitochondria, Parkin is close to PINK1, but no evidence of PINK1 ubiquitination by Parkin or PINK1 phosphorylation by Parkin was found. Co-overexpression of Parkin and PINK1 collapses the normal mitochondrial network into aggregates and perinuclear clusters, often surrounded by autophagic vacuoles. These findings suggest that Parkin and PINK1 modulate mitochondrial trafficking, especially to the perinuclear region, which is associated with autophagy. Mutations in either Parkin or PINK1 may impair this process, leading to defective mitochondrial turnover and neurodegeneration in PD. Protonophores like CCCP induce Parkin translocation to mitochondria. Parkin translocation is PINK1-dependent. PINK1 silencing or knockout prevents Parkin recruitment to depolarized mitochondria. PINK1 overexpression can recruit Parkin to mitochondria even with normal ΔΨm. Parkin and PINK1 co-overexpression causes mitochondrial clustering and autophagy. Parkin and PINK1 do not modify each other, but they collaborate in mitochondrial dynamics. Mitochondrial clustering is microtubule-dependent and involves autophagy. PINK1 and Parkin may regulate mitochondrial trafficking, delivering defective mitochondria to the perinuclear area for degradation. This process is crucial for maintaining mitochondrial health and preventing neurodegeneration in PD.Parkin and PINK1 are key proteins involved in mitochondrial quality control and autophagy in Parkinson's disease (PD). PINK1 and Parkin mutations cause autosomal recessive PD. When mitochondrial membrane potential (ΔΨm) is lost, cytosolic Parkin is recruited to mitochondria, promoting mitochondrial autophagy. This study shows that PINK1 is essential for Parkin recruitment to mitochondria. Overexpression of wild-type (WT) PINK1, but not mutated PINK1, causes Parkin translocation to mitochondria even in cells with normal ΔΨm. Once at mitochondria, Parkin is close to PINK1, but no evidence of PINK1 ubiquitination by Parkin or PINK1 phosphorylation by Parkin was found. Co-overexpression of Parkin and PINK1 collapses the normal mitochondrial network into aggregates and perinuclear clusters, often surrounded by autophagic vacuoles. These findings suggest that Parkin and PINK1 modulate mitochondrial trafficking, especially to the perinuclear region, which is associated with autophagy. Mutations in either Parkin or PINK1 may impair this process, leading to defective mitochondrial turnover and neurodegeneration in PD. Protonophores like CCCP induce Parkin translocation to mitochondria. Parkin translocation is PINK1-dependent. PINK1 silencing or knockout prevents Parkin recruitment to depolarized mitochondria. PINK1 overexpression can recruit Parkin to mitochondria even with normal ΔΨm. Parkin and PINK1 co-overexpression causes mitochondrial clustering and autophagy. Parkin and PINK1 do not modify each other, but they collaborate in mitochondrial dynamics. Mitochondrial clustering is microtubule-dependent and involves autophagy. PINK1 and Parkin may regulate mitochondrial trafficking, delivering defective mitochondria to the perinuclear area for degradation. This process is crucial for maintaining mitochondrial health and preventing neurodegeneration in PD.