Parkinson's kinase LRRK2 phosphorylates a distinct subset of Rabs, and LRRK2-dependent phosphorylation links LRKK2 to ciliogenesis.

The first complete null mutant collection of all rab GTPase genes in a multicellular organism uncovers neuronal development and function sensitive to environmental challenges in Drosophila.

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.

Activating mutations in the leucine-rich repeat kinase 2 cause Parkinson’s disease, and an unbiased genome-wide screen revealed an unexpected, specific role for Rab12 in activating this kinase directly for Rab GTPase phosphorylation.

Rab12 was identified as a key modulator of LRRK2-dependent Rab phosphorylation that mediates the recruitment of LRRK2 to lysosomes in response to damage.

The apical polarity protein CRB3 is crucial for regulating vesicle trafficking in γ-tubulin ring complex assembly during ciliogenesis and cilium-related Hedgehog and Wnt signaling pathways in tumorigenesis.

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.

BDNF-regulated deployment of Rab10 to the distal axon regulates retrograde propagation of neurotrophic signalling, providing a flexible mechanism to fine-tune the communication between the synapse and the cell body of neurons, as well as novel therapeutic targets for neurodegeneration.

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

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.