Abstract
Loss-of function mutations in PTEN-induced putative kinase 1 (PINK1) is one of the most common causes of autosomal recessive Parkinson's disease (PD). PINK1-mediated mitophagy is critical to mitochondrial quality control and plays an important role in PD pathogenesis. Therefore, identifying the regulatory mechanisms of PINK1 expression may provide novel opportunities for PD therapy. Heat-shock protein 70kDa (Hsp70) is involved in neuroprotection as a molecular chaperone in neurodegenerative disorders such as PD. Thus far, the interaction between Hsp70 and PINK1 remains unclear. This study aimed to verify the interaction between Hsp70 and PINK1, as well as the role of Hsp70 in PINK1 stability, cell autophagy, and PINK1-mediated mitophagy. The interaction and subcellular location of Hsp70 and PINK1 were verified by coimmunoprecipitation and immunofluorescence colocalization. Western blot analysis was used to determine the role of Hsp70 in PINK1 stability. Immunofluorescence and Western blot analyses were performed to determine the role of Hsp70 in PINK1-mediated mitophagy. We identified the interaction between Hsp70 and PINK1 and revealed that Hsp70 stabilized PINK1 by decreasing PINK1 degradation. Our data demonstrated that Hsp70 participated in PINK1-mediated mitophagy. Hsp70participated in PINK1-mediated mitophagy by stabilizing PINK1.
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