The endosomal GEF Mon1-Ccz1 binds to Atg8 on autophagosomes, and recruits its substrate, the Rab7-like Ypt7, which then mediates fusion of the autophagosomes with the lysosome.

Analysis of the Arabidopsis V-ATPase reveals convergent evolution of differential targeting as well as redundancy of the endosomal and vacuolar isoforms during vegetative development.

DNA nanodevices can be targeted to specific cell types in Caenorhabditis elegans with subcellular precision by exploiting either endogenous or synthetic receptors.

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.

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.

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.

The USP-50/USP8 protease removes the Rab5 GEF Rabex5 from endosomes while facilitating recruitment of the Rab7 GEF SAND-1/Mon1, promoting endosome maturation.

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.

The RAB-28 GTPase regulates ciliary extracellular vesicle shedding, which may be important for neuron-glia communication.

SiR does not revert to wild type when produced in high-TEVp cell lines, is non-toxic in vivo, maintains transsynaptic spreading capabilities and revertant mutations do not accumulate during in vivo experiments.