The ciliary G-protein Arl13B – which is often mutated in Joubert syndrome – is the Guanine nucleotide exchange factor for the G-protein Arl3 and exclusively localizes to cilia.

High-resolution proteomics in conjunction with biochemical and electrophysiological experiments revealed that the channel-kinase TRPM7 in rodent brain forms macromolecular complexes containing the metal transporters CNNM1-4 and a small G-protein ARL15.

The active small G protein, Arl15-GTP, interacts with the MH2 domain of Smad4 and positively regulates the TGFß family signaling pathway by promoting the assembly of the Smad-complex.

The ability of epithelial cells to distinguish between domains on opposing cell surfaces within a tissue, a property known as planar cell polarity, relies on proteins and protein complexes directing the traffic of signaling proteins to specific locations on the cell surface membrane.

BART is a co-GEF for ARL3 and maintains the active ARL3-GTP until it is recycled by ARL3 effectors.

ADP-ribosylation factor-like GTPase 15, an atypical small GTPase, binds to cystathionine-β-synthase-pair domain divalent metal cation transport mediator (CNNM) membrane proteins to inhibit divalent cation efflux by CNNM proteins and influx by transient receptor potential ion channel subfamily M member 7.

Discovery and characterisation of a novel allosteric inhibitor-binding site in human Bloom syndrome protein.

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

A Tubby protein regulates ciliary membrane morphology and phosphoinositide composition in a context-dependent manner.

Apicomplexan-like parasites originated several times independently and many of them contain cryptic plastid organelles, which demonstrate that the parasites evolved from photosynthetic algae.