Polycystic Kidney Disease 2-Like 1 Proteins (PKD2L1)

Zebrafish Polycystic Kidney Disease 2-Like 1 (PKD2L1) interaction partners

1. cerebrospinal fluid (CSF)-contacting neurons are mechanosensory cells whose Pkd2l1-driven spontaneous activity reflects CSF flow in vivo.

Mouse (Murine) Polycystic Kidney Disease 2-Like 1 (PKD2L1) interaction partners

1. The pore helix and transmembrane segment 6 of PKD2L1 are involved in upper and lower-gate opening, adopt an open conformation.

2. In epileptic seizures mouse model, Pkdl deficiency leads to the loss of beta2AR on neuronal cilia, reduction in cAMP levels in the central nervous system, and reduction in the activation of cAMP response element-binding protein.

3. This study demonstrated that spontaneously active unitary currents in CSF-cNs are due to PKD2L1 channels that are capable, with a single opening, of triggering action potentials

4. sour taste cells in the posterior tongue express a proton current; the current is present in PKD2L1-expressing taste cells from circumvallate, foliate, and fungiform papillae but not in a variety of other cells

5. findings suggest that PKD2L1 partly contributes to sour taste responses in mice and that receptors other than PKDs would be involved in sour detection

6. All channel-forming isoforms of TRPP channels (polycystin-2, polycystin-L, and polycystin-2L2) were expressed in adult mouse lacrimal gland.

7. These results demonstrate that Asp(523) in PKD2L1 is a key determinant of Ca(2+) permeation into the PKD1L3/PKD2L1 complex and that PKD2L1 contributes to forming the pore of the PKD1L3/PKD2L1 channel.

8. the PKD2L1-PKD1L3 complex is involved in acid sensing in vivo

9. PKD2L1 forms functional cation channels on the plasma membrane by interacting with PKD1

10. Pkd1l3 and Pkd2l1 are co-expressed in a select subset of taste receptor cells and therefore may, like other PKD channels, function as a heteromer.

11. These results suggest that PKD1L3 and PKD2L1 heteromers may function as sour taste receptors.

12. Animals lacking PKD2L1-expressing cells are completely devoid of taste responses to sour stimuli.

13. The taste receptor PKD2L1 is expressed by type III taste cells, but not by type I and II cells, in the mouse taste bud.

14. The off-response property of PKD1L3-PKD2L1 channels might explain the physiological phenomena occurring during sour taste sensation.

15. Results demonstrate that TRPP3, on its own, can act as a voltage-dependent, pH- and volume-sensitive plasma membrane cation channel.

16. PKD1L3-PKD2L1 channel activation by acetic acid was pH-dependent and occurred when the ambient pH was <3.1.

Human Polycystic Kidney Disease 2-Like 1 (PKD2L1) interaction partners

1. Charge-neutralizing mutations (K452Q, K455Q and K461Q) in transmembrane segment 4 reduced gating charges, positively shifted the Boltzmann-type activation curve [i.e., open probability (P open)-V curve] and altered the time-courses of activation/deactivation of PKD2L1, indicating that this region constitutes part of a voltage sensor.

2. The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics. Here the authors show that these differences are reflected in the architecture of polycystin 2-l1.

3. Clustered phosphorylation sites, Ser-682, Ser-685, and Ser-686 are significant for the channel regulation by phosphorylation.

4. The pore helix and transmembrane segment 6 of PKD2L1 are involved in upper and lower-gate opening, adopt an open conformation.

5. PKD2 and PKD1 genes are mutated in autosomal dominant polycystic kidney disease. PKD2 can form either a homomeric cation channel or a heteromeric complex with the PKD1 receptor, presumed to respond to ligand(s) and/or mechanical stimuli. Here, we identify a two-residue hydrophobic gate in PKD2L1, and a single-residue hydrophobic gate in PKD2.

6. palmitoylation at Cys-38 and phosphorylation at Thr-39 independently regulated TRPP3 channel function

7. our study identified C1 as the first PKD2L1 domain essential for both PKD2L1 trimerization and channel function, and suggest that PKD2L1 and PKD2L1/PKD1L3 channels share the PKD2L1 trimerization process.

8. Trimerization may be important for both homo- and possibly heteromeric assemblies of PKD2L1.

9. This study demonistrated that human PKD2L play the role of food preference behavior.

10. Pkd2L1 is a novel target channel whose function is regulated by the versatile scaffolding protein RACK1.

11. Despite the moderate sequence identity between C-terminal regulatory domains (CRDs) of PKD2 and PKD2L1, they both form trimers, implying that trimeric organization of CRDs may be true of all polycystin channels.

12. the PKD2L1-PKD1L3 complex is involved in acid sensing in vivo

13. The calcium-binding EF-hand in polycystin-L is not a domain for channel activation and ensuing inactivation.

14. Taken together, alpha-actinin not only attaches TRPP3 to the cytoskeleton but also up-regulates TRPP3 channel function.