The atomic resolution cryo-EM structure of somatostatin receptor 2 (SSTR2) provides insights into the mechanism by which SSTRs recognize their ligands and will serve as a platform to develop selective agonists and therapeutics.

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

Membrane receptor proteins move through primary cilia largely by passive diffusion rather than by active intraflagellar transport.

Direct patch clamp of ependymal motile cilia reveals that voltage-gated calcium channels in the cell body dominate their electrical and calcium signaling properties.

Six BBS proteins form a core BBSome transport vehicle, which is sufficient for recognizing membrane proteins for transport into the ciliary compartment.

Pathogenic LRRK2kinase requires Rab10 and RILPL1 to block primary cilia formation, shortening cilia on cholinergic neurons needed for a hedgehog driven circuit that supports dopaminergic neurons in mouse brain.

The mechanism of signaling receptor delivery to primary cilia involves a specific cellular role of a Rab protein that is critical for vertebrate development.

Genetic knock-outs of the dynein-2 intermediate chains reveals that both are essential for correct cilia function and transition zone organization, but play different functions in the assembly of dynein-2 motor and in primary cilia formation.

Trafficking of optogenetic tools to primary cilia using nanobodies allows to study cAMP signaling with spatial and temporal resolution independent of the cell body.