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The primary cilia polycystin proteins, polycystin-1 and polycystin-2, affect cilia length in the kidney collecting duct epithelia, but only polycystin-2 is required for the functional ion channel in this organelle.

Signaling at the primary cilium is important to sustain the morphology, connectivity, and survival of a key neural population within the brain.

Bardet–Biedl syndrome 3 (BBS3) protein promotes phospholipase D to load onto the BBSome at the ciliary tip for moving out of the cilium via intraflagellar transport.

Two cryo-EM structures of the mammalian BBSome show how the BBSome is recruited to membranes and activated by the GTPase ARL6 prior to binding transmembrane proteins.

Smurf1 and Smurf2 have essential functions in the mammalian Shh signaling pathway, binding to and ubiquitylating Patched1, leading to its endocytosis and subsequent degradation in lysosomes.

Trisomy 21, the genetic cause of Down syndrome, produces elevated centrosome protein levels reducing intracellular trafficking to and from the centrosome thereby delaying primary ciliogenesis, ciliary signaling, and mouse cerebellar development.

An anchored phosphatase-deacetylase complex participates in primary cilia development.

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.

The apical polarity protein CRB3 is crucial for regulating vesicle trafficking in γ-tubulin ring complex assembly during ciliogenesis and cilium-related Hedgehog and Wnt signaling pathways in tumorigenesis.

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