Activation of Ca²⁺ phosphatase Calcineurin regulates Parkin translocation to mitochondria and mitophagy in flies.

ABSTRACT: Selective removal of dysfunctional mitochondria via autophagy is crucial for the maintenance of cellular homeostasis. This event is initiated by the translocation of the E3 ubiquitin ligase Parkin to damaged mitochondria, and it requires the Serine/Threonine-protein kinase PINK1. In a coordinated set of events, PINK1 operates upstream of Parkin in a linear pathway that leads to the phosphorylation of Parkin, Ubiquitin, and Parkin mitochondrial substrates, to promote ubiquitination of outer mitochondrial membrane proteins. Ubiquitin-decorated mitochondria are selectively recruiting autophagy receptors, which are required to terminate the organelle via autophagy. In this work, we show a previously uncharacterized molecular pathway that correlates the activation of the Ca²⁺-depende

SUBMITTER: Marchesan E 

PROVIDER: S-EPMC10850161 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature