Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B . Both PKD1 and PKD2 are required for channel activity . Involved in renal tubulogenesis . Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (By similarity). Acts as a regulator of cilium length, together with PKD2 (By similarity). The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling (By similarity). The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling (By similarity). May be an ion-channel regulator. Involved in adhesive protein-protein and protein-carbohydrate interactions. Likely to be involved with polycystin-1-interacting protein 1 in the detection, sequestration and exocytosis of senescent mitochondria .
Subcellular locations: Cell membrane, Cell projection, Cilium, Endoplasmic reticulum, Golgi apparatus, Vesicle, Secreted, Extracellular exosome
PKD1 localization to the plasma and ciliary membranes requires PKD2, is independent of PKD2 channel activity, and involves stimulation of PKD1 autoproteolytic cleavage at the GPS domain. PKD1:PKD2 interaction is required to reach the Golgi apparatus from endoplasmic reticulum and then traffic to the cilia (By similarity). Ciliary localization of PKD1 requires BBS1 and ARL6/BBS3 (By similarity). Cell surface localization requires GANAB . Detected on migrasomes and on extracellular exosomes in urine .