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

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

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.

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

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.

Parkinson’s disease-associated LRRK2 kinase is recruited to membranes by its Rab GTPase substrates, and LRRK2 is both retained on membranes and further activated there by cooperative interaction with the phosphorylated Rab proteins that it generates.

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.

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.

Multicellular and socially aggregating prokaryotes contain previously undescribed, chaperone-based systems predicted to mediate defensive biological conflicts, several components of which are thematically similar antecedents of eukaryotic apoptosis pathways.

In lateral roots, cells employ a novel pathway to cell edges to control directional growth, which acts independently of the leading paradigm of oriented deposition of cellulose microfibrils at faces.