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.
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.
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.
Comparative genetics between distant plant species shows that for the PIN auxin transport proteins differential membrane and tissue-level accumulation, transport activity, and interaction result in different functional properties in the shoot post transcription.