PKD2L1 Antibody

1. The pore helix and transmembrane segment 6 of PKD2L1 are involved in upper and lower-gate opening, adopt an open conformation. PMID: 29567962
2. 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. PMID: 29899465
3. palmitoylation at Cys-38 and phosphorylation at Thr-39 independently regulated TRPP3 channel function PMID: 27754867
4. 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. PMID: 25820328
5. Trimerization may be important for both homo- and possibly heteromeric assemblies of PKD2L1. PMID: 22193359
6. This study demonistrated that human PKD2L play the role of food preference behavior. PMID: 22794107
7. Pkd2L1 is a novel target channel whose function is regulated by the versatile scaffolding protein RACK1. PMID: 22174419
8. 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. PMID: 20408813
9. the PKD2L1-PKD1L3 complex is involved in acid sensing in vivo PMID: 20406802
10. The calcium-binding EF-hand in polycystin-L is not a domain for channel activation and ensuing inactivation. PMID: 11959145
11. Taken together, alpha-actinin not only attaches TRPP3 to the cytoskeleton but also up-regulates TRPP3 channel function. PMID: 17944866

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HGNC: 9011

OMIM: 604532

KEGG: hsa:9033

STRING: 9606.ENSP00000325296

UniGene: Hs.159241