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10.1083/jcb.200605093 http://scihub22266oqcxt.onion/10.1083/jcb.200605093 17190791!2063630!17190791     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Cell+Biol 2007 ; 176 (1): 89-100 Nephropedia Template TP {{tp|p=17190791|t=2007. Regulation of activity and localization of the WNK1 protein kinase by hyperosmotic stress |pdf=|usr=}}{{17190791}} gab.com Text Regulation of activity and localization of the WNK1 protein kinase by hyperosmotic stress JO: J Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=17190791 #FOAvip Mutations within the WNK1 (with-no-K[Lys] kinase-1) gene cause Gordon's hypertension syndrome. Little is known about how WNK1 is regulated. We demonstrate that WNK1 is rapidly activated and phosphorylated at multiple residues after exposure of cells to hyperosmotic conditions and that activation is mediated by the phosphorylation of its T-loop Ser382 residue, possibly triggered by a transautophosphorylation reaction. Activation of WNK1 coincides with the phosphorylation and activation of two WNK1 substrates, namely, the protein kinases STE20/SPS1-related proline alanine-rich kinase (SPAK) and oxidative stress response kinase-1 (OSR1). Small interfering RNA depletion of WNK1 impairs SPAK/OSR1 activity and phosphorylation of residues targeted by WNK1. Hyperosmotic stress induces rapid redistribution of WNK1 from the cytosol to vesicular structures that may comprise trans-Golgi network (TGN)/recycling endosomes, as they display rapid movement, colocalize with clathrin, adaptor protein complex 1 (AP-1), and TGN46, but not the AP-2 plasma membrane-coated pit marker nor the endosomal markers EEA1, Hrs, and LAMP1. Mutational analysis suggests that the WNK1 C-terminal noncatalytic domain mediates vesicle localization. Our observations shed light on the mechanism by which WNK1 is regulated by hyperosmotic stress. Twit Text FOAVip Regulation of activity and localization of the WNK1 protein kinase by hyperosmotic stress ????J Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=17190791 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=17190791 #FOAvip English Wikipedia <ref>{{Cite pmid|17190791}}</ref> Regulation of activity and localization of the WNK1 protein kinase by hyperosmotic stress #MMPMID17190791 Zagorska A; Pozo-Guisado E; Boudeau J; Vitari AC; Rafiqi FH; Thastrup J; Deak M; Campbell DG; Morrice NA; Prescott AR; Alessi DR J Cell Biol 2007[Jan]; 176 (1): 89-100 PMID17190791show ga Mutations within the WNK1 (with-no-K[Lys] kinase-1) gene cause Gordon's hypertension syndrome. Little is known about how WNK1 is regulated. We demonstrate that WNK1 is rapidly activated and phosphorylated at multiple residues after exposure of cells to hyperosmotic conditions and that activation is mediated by the phosphorylation of its T-loop Ser382 residue, possibly triggered by a transautophosphorylation reaction. Activation of WNK1 coincides with the phosphorylation and activation of two WNK1 substrates, namely, the protein kinases STE20/SPS1-related proline alanine-rich kinase (SPAK) and oxidative stress response kinase-1 (OSR1). Small interfering RNA depletion of WNK1 impairs SPAK/OSR1 activity and phosphorylation of residues targeted by WNK1. Hyperosmotic stress induces rapid redistribution of WNK1 from the cytosol to vesicular structures that may comprise trans-Golgi network (TGN)/recycling endosomes, as they display rapid movement, colocalize with clathrin, adaptor protein complex 1 (AP-1), and TGN46, but not the AP-2 plasma membrane-coated pit marker nor the endosomal markers EEA1, Hrs, and LAMP1. Mutational analysis suggests that the WNK1 C-terminal noncatalytic domain mediates vesicle localization. Our observations shed light on the mechanism by which WNK1 is regulated by hyperosmotic stress. |Amino Acid Sequence[MESH] |Animals[MESH] |Catalytic Domain/drug effects[MESH] |Cell Survival/drug effects[MESH] |Clathrin/metabolism[MESH] |Cytoplasmic Vesicles/drug effects/enzymology[MESH] |Enzyme Activation/drug effects[MESH] |HeLa Cells[MESH] |Humans[MESH] |Intracellular Signaling Peptides and Proteins[MESH] |Minor Histocompatibility Antigens[MESH] |Molecular Sequence Data[MESH] |Osmotic Pressure[MESH] |Phosphorylation/drug effects[MESH] |Phosphoserine/metabolism[MESH] |Protein Binding/drug effects[MESH] |Protein Serine-Threonine Kinases/chemistry/*metabolism[MESH] |Protein Transport/drug effects[MESH] |Rats[MESH] |Recombinant Fusion Proteins/metabolism[MESH] |Sorbitol/*pharmacology[MESH]Regulation of activity and localization of the WNK1 protein kinase by (epmc).pdf DeepDyve Pubget Overpricing