Serine/Threonine kinase PINK1 (PTEN-induced putative kinase protein 1) plays a critical role in preventing mitochondrial dysfunction during cellular stress. PINK is translated in the cytosol, then translocated to the outer mitochondrial membrane where it is rapidly cleaved and degraded as a part of normal mitochondrial function. In damaged (depolarized) mitochondria PINK becomes stabilized and accumulates, resulting in the subsequent phosphorylation of numerous proteins on the mitochondrial surface including Mfn2. Ultimately PARK2 (E3 Ubiquitin Ligase Parkin) is recruited to the damaged mitochondria where it is activated by 1) PINK-mediated phosphorylation of PARK2 at serine 65, and 2) PARK2 interaction with phosphorylated Ubiquitin (also phosphorylated by PINK on serine 65). This signaling cascade is critical for clearing the damaged mitochondria via selective autophagy (mitophagy) by mediating activation and translocation of PARK2.
Recombinant human PINK1 is not active in vitro, while this protein from the Red Flour Beetle (Tribolium castaneum) effectively phosphorylates recombinant Parkin, mono-Ubiquitin, and poly-Ubiquitin chains. It specifically phosphorylates both Parkin and Ubiquitin at serine 65. This recombinant protein contains N-terminal 6-His and MBP tags.
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