King Rail (Rallus elegans) presence in the Midwestern United States is predicted by local-scale factors and avian community.

The King Rail (Rallus elegans) is a wetland dependent species of conservation concern. Our objective was to gain a better understanding of the breeding habitat associations of King Rails in the Midwestern United States and the relationship of this species to other obligate marsh birds using occupancy and MaxEnt models. To collect data pertaining to occupancy, we placed trail cameras at 50 random points in coastal wetlands in the western Lake Erie basin where calls of King Rails were continuously broadcast at night. Data pertaining to other marsh bird species were collected via call-broadcast surveys and camera surveys at each sample point. For MaxEnt modeling, we obtained presence data for King Rails and other obligate marsh birds from eBird and habitat data from GIS databases. Trail cameras and call-broadcast surveys captured 10 detections of King Rails at nine sites, an 18% naive occupancy rate. King Rail occupancy was positively related to amount of interspersion, average water depth, and percent cover of emergent vegetation at local scales within a 5-m radius. Our MaxEnt models indicated that, at a broader scale, the presence of other rail species such as the Sora (Porzana carolina) may be more important for predicting King Rail presence than other marsh birds or coarse wetland categories such as "emergent vegetation." Our results could help wetland managers to predict where King Rails occur and to adapt management plans to incorporate King Rail conservation.

Polycystin-1, STAT6, and P100 function in a pathway that transduces ciliary mechanosensation and is activated in polycystic kidney disease.

Primary cilia are implicated in the pathogenesis of autosomal-dominant polycystic kidney disease (ADPKD), which results from defects in polycystin-1 (PC1), but the function of PC1 remains poorly understood. Here, we show that PC1 undergoes proteolytic cleavage that results in nuclear translocation of its cytoplasmic tail. The PC1 tail interacts with the transcription factor STAT6 and the coactivator P100, and it stimulates STAT6-dependent gene expression. Under normal conditions, STAT6 localizes to primary cilia of renal epithelial cells. Cessation of apical fluid flow results in nuclear translocation of STAT6. Cyst-lining cells in ADPKD exhibit elevated levels of nuclear STAT6, P100, and the PC1 tail. Exogenous expression of the human PC1 tail results in renal cyst formation in zebrafish embryos. These results identify a novel mechanism of cilia function in the transduction of a mechanical signal to changes of gene expression involving PC1 and show that this pathway is inappropriately activated in ADPKD.

Identification of an N-terminal glycogen synthase kinase 3 phosphorylation site which regulates the functional localization of polycystin-2 in vivo and in vitro.

PKD2 is mutated in 15% of patients with autosomal dominant polycystic kidney disease. Polycystin-2 (PC2), the PKD2 protein, is a non-selective Ca(2+)-permeable cation channel which may function at the cell surface and ER. Nevertheless, the factors that regulate the dynamic translocation of PC2 between the ER and other compartments are not well understood. Constitutive phosphorylation of PC2 at a single C-terminal site (Ser(812)) has been previously reported. As we were unable to abolish phospholabelling of PC2 in HEK293 cells by site-directed mutagenesis of Ser(812) or all five predicted phosphorylation sites in the C-terminus, we hypothesized that PC2 could also be phosphorylated at the N-terminus. In this paper, we report the identification of a new phosphorylation site for PC2 within its N-terminal domain (Ser(76)) and demonstrate that this residue is phosphorylated by glycogen synthase kinase 3 (GSK3). The consensus recognition sequence for GSK3 (Ser(76)/Ser(80)) is evolutionarily conserved down to lower vertebrates. In the presence of specific GSK3 inhibitors, the lateral plasma membrane pool of endogenous PC2 redistributes into an intracellular compartment in MDCK cells without any change in primary cilia localization. Finally, co-injection of wild-type but not a S76A/S80A mutant PKD2 capped mRNA could rescue the cystic phenotype induced by an antisense morpholino oligonucleotide to pkd2 in zebrafish pronephric kidney. We conclude that surface localization of PC2 is regulated by phosphorylation at a unique GSK3 site in its N-terminal domain in vivo and in vitro. This site is functionally significant for the maintenance of normal glomerular and tubular morphology.