The structure of human PINK1 explains structural regulation and clarity on the impact of loss of function disease-associated mutations, which may stimulate future drug discovery efforts for both familial and idiopathic Parkinson's disease.

By reducing mitochondrial fusion, MUL1 compensates for the mutations in PINK1 or parkin that underlie certain cases of Parkinson's disease.

Mitophagy occurs in Drosophila flight muscle and dopaminergic neurons in vivo and increases with aging in a PINK1/parkin-dependent fashion.

A crucial step during the mitophagy cascade involves the disassembly of connections between mitochondria and the endoplasmic reticulum via the retrotranslocation of Mfn2 tethering complexes by the Parkinson's disease genes PARKIN and PINK1, as well as the ATPase VCP/p97.

In vitro and in vivo data show that C-natriuretic peptide is significant for increasing mitochondrial bioenergetics by cAMP-PKA pathway and improving cytoplasmic and nuclear maturation of maternally aged oocyte.

Caenorhabditis elegans utilize multiple strategies to optimize germline mitochondrial genome integrity at the foundational stage of gonad development.

Models that generate tandem alignments of cell polarities are more readily compatible with the formation of PIN1 polarity patterns in plant leaf buds than the most widely accepted “up-the-gradient” model.

Investigations of binding of the scaffold protein PICK1 to transmembrane proteins in their native membrane environment demonstrate potent but slow dynamics and reveal distinct binding modes supporting different biological functions.

Two GAP proteins bound to mitochondria regulate the enyzme Rab7, and thereby the expansion of the isolation membrane during mitophagy, downstream of PINK1 and Parkin, two proteins that are mutated in familial Parkinson's disease.

The hormonal circuitry controlling development in plants can be studied and re-programmed with hormone activated Cas9-based repressors.