In Vitro Comparison of the Activity Requirements and Substrate Specificity of Human and Triboleum castaneum PINK1 Orthologues.

ABSTRACT: Mutations in the gene encoding the mitochondrial kinase PINK1 cause early-onset familial Parkinson's disease. To understand the biological function of PINK1 and its role in the pathogenesis of Parkinson's disease, it is useful to study its kinase activity towards substrates both in vivo and in vitro. For in vitro kinase assays, a purified Triboleum castaneum PINK1 insect orthologue is often employed, because it displays higher levels of activity when compared to human PINK1. We show, however, that the activity requirements, and more importantly the substrate specificity, differ between both orthologues. While Triboleum castaneum PINK1 readily phosphorylates the PINKtide peptide and Histone H1 in vitro, neither of these non-physiological substrates is phosphorylated by human PINK1. Nonethel

SUBMITTER: Aerts L 

PROVIDER: S-EPMC4718624 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature