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.

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

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.

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.

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.

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.

Neuropeptidergic signaling via cilia-localized receptors dynamically regulates excitatory synaptic drive in postnatal rat neocortical pyramidal neurons.

Four conserved ciliary localization signals in the Joubert syndrome-associated INPP5E phosphoinositide phosphatase control its ciliary accumulation.

Electron tomography and biochemical approaches demonstrate a direct role for WDR35, beyond integrity of the IFT-A holocomplex, in the formation and fusion of electron-dense-coated vesicles to the ciliary sheath and pocket for delivery of cargos necessary for axoneme elongation.

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.