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.

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

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

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.

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.

PPM1H protein phosphatase dephosphorylates Rab proteins modulating LRRK2 signalling.

CapZ controls actin filament density around immature early endosomes via its C-terminal domain to facilitate the homotypic fusion of the endocytic vesicles, and it functions as a scaffold protein via its N-terminal domain to recruit RAB5 effectors to early endosomes.

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.

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.