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.

Parkin ubiquitination of damaged mitochondria recruits the Rab GEF, RABGEF1, to regulate downstream Rab cycles and ATG9A recruitment to growing phagophores that are participating in mitophagy.

An image-based multiplex autophagosome RNAi screen targeting all Rab GTPases as well as their GAPs and GEFs identifies the Rab GEF SMCR8 as multifaceted autophagy modulator, which regulates kinase activity and gene expression of ULK1.

Vps29 promotes retromer localization in the adult Drosophila brain, engaging Rab7 and TBC1D5, and its loss triggers age-dependent neuronal impairments in endolysosomal trafficking and synaptic transmission.

Introducing a hominoid-specific gene into mice induces cortical folding.

Relocation of Rab, Ras and Rho family GTPases to the surface of mitochondria enables efficient identification of their effectors, exchange factors and GAPs by proximity biotinylation.

Rhythmic transcriptome analyses of human skeletal muscle tissue and cultured primary myotubes reveal an essential role for the circadian coordination of glucose homeostasis and lipid metabolism in human skeletal muscle.

A microRNA prevents the accumulation of toxic proteins by inducing autophagy.

The uniparental inheritance of mammalian mitochondria results from elimination of paternal mitochondria by a mitophagic process that requires the E3 ubiquitin ligases PARKIN and MUL1.

Analysis of multiple guanine exchange factors shows that Rab activation can occur via a number of mechanistically distinct GDP-release pathways.