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10.1073/pnas.1902042116 http://scihub22266oqcxt.onion/10.1073/pnas.1902042116 31488724!6754598!31488724     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2019 ; 116 (38): 19176-19186 Nephropedia Template TP {{tp|p=31488724|t=2019. Phosphorylated claudin-16 interacts with Trpv5 and regulates transcellular calcium transport in the kidney |pdf=|usr=}}{{31488724}} gab.com Text Phosphorylated claudin-16 interacts with Trpv5 and regulates transcellular calcium transport in the kidney JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=31488724 #FOAvip Familial hypomagnesemia with hypercalciuria and nephrocalcinosis (FHHNC) was previously considered to be a paracellular channelopathy caused by mutations in the claudin-16 and claudin-19 genes. Here, we provide evidence that a missense FHHNC mutation c.908C>G (p.T303R) in the claudin-16 gene interferes with the phosphorylation in the claudin-16 protein. The claudin-16 protein carrying phosphorylation at residue T303 is localized in the distal convoluted tubule (DCT) but not in the thick ascending limb (TAL) of the mouse kidney. The phosphomimetic claudin-16 protein carrying the T303E mutation but not the wildtype claudin-16 or the T303R mutant protein increases the Trpv5 channel conductance and membrane abundance in human kidney cells. Phosphorylated claudin-16 and Trpv5 are colocalized in the luminal membrane of the mouse DCT tubule; phosphomimetic claudin-16 and Trpv5 interact in the yeast and mammalian cell membranes. Knockdown of claudin-16 gene expression in transgenic mouse kidney delocalizes Trpv5 from the luminal membrane in the DCT. Unlike wildtype claudin-16, phosphomimetic claudin-16 is delocalized from the tight junction but relocated to the apical membrane in renal epithelial cells because of diminished binding affinity to ZO-1. High-Ca(2+) diet reduces the phosphorylation of claudin-16 protein at T303 in the DCT of mouse kidney via the PTH signaling cascade. Knockout of the PTH receptor, PTH1R, from the mouse kidney abrogates the claudin-16 phosphorylation at T303. Together, these results suggest a pathogenic mechanism for FHHNC involving transcellular Ca(2+) pathway in the DCT and identify a molecular component in renal Ca(2+) homeostasis under direct regulation of PTH. Twit Text FOAVip Phosphorylated claudin-16 interacts with Trpv5 and regulates transcellular calcium transport in the kidney ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=31488724 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=31488724 #FOAvip English Wikipedia <ref>{{Cite pmid|31488724}}</ref> Phosphorylated claudin-16 interacts with Trpv5 and regulates transcellular calcium transport in the kidney #MMPMID31488724 Hou J; Renigunta V; Nie M; Sunq A; Himmerkus N; Quintanova C; Bleich M; Renigunta A; Wolf MTF Proc Natl Acad Sci U S A 2019[Sep]; 116 (38): 19176-19186 PMID31488724show ga Familial hypomagnesemia with hypercalciuria and nephrocalcinosis (FHHNC) was previously considered to be a paracellular channelopathy caused by mutations in the claudin-16 and claudin-19 genes. Here, we provide evidence that a missense FHHNC mutation c.908C>G (p.T303R) in the claudin-16 gene interferes with the phosphorylation in the claudin-16 protein. The claudin-16 protein carrying phosphorylation at residue T303 is localized in the distal convoluted tubule (DCT) but not in the thick ascending limb (TAL) of the mouse kidney. The phosphomimetic claudin-16 protein carrying the T303E mutation but not the wildtype claudin-16 or the T303R mutant protein increases the Trpv5 channel conductance and membrane abundance in human kidney cells. Phosphorylated claudin-16 and Trpv5 are colocalized in the luminal membrane of the mouse DCT tubule; phosphomimetic claudin-16 and Trpv5 interact in the yeast and mammalian cell membranes. Knockdown of claudin-16 gene expression in transgenic mouse kidney delocalizes Trpv5 from the luminal membrane in the DCT. Unlike wildtype claudin-16, phosphomimetic claudin-16 is delocalized from the tight junction but relocated to the apical membrane in renal epithelial cells because of diminished binding affinity to ZO-1. High-Ca(2+) diet reduces the phosphorylation of claudin-16 protein at T303 in the DCT of mouse kidney via the PTH signaling cascade. Knockout of the PTH receptor, PTH1R, from the mouse kidney abrogates the claudin-16 phosphorylation at T303. Together, these results suggest a pathogenic mechanism for FHHNC involving transcellular Ca(2+) pathway in the DCT and identify a molecular component in renal Ca(2+) homeostasis under direct regulation of PTH. |*Transcytosis[MESH] |Animals[MESH] |Calcium Channels/genetics/*metabolism[MESH] |Calcium/*metabolism[MESH] |Cell Membrane Permeability[MESH] |Claudins/antagonists & inhibitors/genetics/*metabolism[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Kidney Tubules, Distal/*metabolism[MESH] |Male[MESH] |Mice[MESH] |Mice, Knockout[MESH] |Phosphorylation[MESH] |TRPV Cation Channels/antagonists & inhibitors/genetics/*metabolism[MESH]Phosphorylated claudin-16 interacts with Trpv5 and regulates transcell(epmc).pdf DeepDyve Pubget Overpricing