Soluble fragments cleaved from the N-terminus of PC-1 activate the PC-1/PC-2 heteromeric polycystin channel, describing for the first time that the N-terminus itself is an endogenous ligand.

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.

The selectivity characteristics of PC-2L1, which make it a principal source of calcium in primary cilia function, is presented and advances understanding of the similarity and differences of TRPP ion channels.

The Platynereis startle circuit links polycystin-dependent hydrodynamic sensors to muscle and ciliary effector cells.

PKD2 (polycystin-2) channels are a major component of a flow-sensing signaling mechanism in endothelial cells that stimulates vasodilation and reduces blood pressure.

Outward calcium ion currents desensitize the human PKD2-L1 ion channel via a mechanism that is independent of cytosolic motifs.

Three-dimensional imaging was used to identify structural and quantitative features of developing lymphatics in the kidneys of mice, humans and in a genetic mouse model of polycystic kidney disease.

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

Arterial myocyte PKD2 channels are activated by vasoconstrictor stimuli, which increases blood pressure, are upregulated during hypertension and cell-specific knockout in vivo reduces both physiological blood pressure and hypertension.