Analyses of a developmentally regulated Drosophila myofiber remodeling program provide insight into induced autophagy required for T-tubule membrane reorganization, and uncover a conserved Rab2 role in autophagosome-lysosome fusion.

Experiments in C. elegans reveal how synaptotagmin and Rab3, the 'yin and yang' of synapses, control whether transmitter vesicles remain docked at the presynaptic membrane or release their contents into the synapse.

With monoubiquitination sites of Rab5 identified and structural and biochemical studies using chemically synthesized ubiquitinated Rab5, Rab5 monoubiquitination is found to downregulate the function of Rab5 in a site-dependent manner.

Rab6A binds directly to both the C-terminus and the N-terminal motor domain of the kinesin KIF1C to regulate vesicle motility and Golgi organization.

A human three-helix Rab-binding domain can potentially bind to two Rab proteins simultaneously with different affinities at binding sites generated by gene duplication.

Rab26 selectively directs synaptic and secretory vesicles into preautophagosomal structures, suggesting the presence of a novel pathway (vesiculophagy) for degradation of synaptic vesicles.

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

Both protein-protein and protein-lipid interactions are essential for Rab5 symmetry breaking at the early endosome.

Discovery of a physiological LRRK2 substrate and a new mechanism of Rab regulation should aid Parkinson’s research and the understanding of Rab function.

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.