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.

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

Dominant mutations in Arl3, linked to inherited retinal dystrophy, disrupt the active Arl3-GTP ciliary gradient and cause a defect in rod photoreceptor nuclear migration that can be rescued by elevating ciliary Arl3 activity or reducing aberrant non-ciliary Arl3 activity.

Soluble αβ-tubulin assembly is regulated by a cage-like molecular complex containing tubulin cofactors and Arl2.

The areas of the cerebral cortex that are necessary for mice to perform goal-directed navigation differ depending on previous experience in cognitively challenging tasks.

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.

ARH3 is an enzyme that hydrolyses serine ADP-ribosylation, a recently uncovered post-translational protein modification.

ARL13B regulates cell ciliation and cilia length from within cilia and Sonic hedgehog response from outside of cilia indicating the two processes can be spatially uncoupled.

Membrane recruitment of BBSome is coupled to a conformational change, and interaction of the BBSome with GPCR cargoes depends on the GPCRs releasing their amphipathic helix 8 from the membrane.

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.