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10.1042/BJ20061850 http://scihub22266oqcxt.onion/10.1042/BJ20061850 17341212!1925243!17341212     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 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochem+J 2007 ; 405 (1): 85-93 Nephropedia Template TP {{tp|p=17341212|t=2007. Regulation of the renal-specific Na+-K+-2Cl- co-transporter NKCC2 by AMP-activated protein kinase (AMPK) |pdf=|usr=}}{{17341212}} gab.com Text Regulation of the renal-specific Na+-K+-2Cl- co-transporter NKCC2 by AMP-activated protein kinase (AMPK) JO: Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=17341212 #FOAvip The renal-specific NKCC2 (Na+-K+-2Cl- co-transporter 2) is regulated by changes in phosphorylation state, however, the phosphorylation sites and kinases responsible have not been fully elucidated. In the present study, we demonstrate that the metabolic sensing kinase AMPK (AMP-activated protein kinase) phosphorylates NKCC2 on Ser126 in vitro. Co-precipitation experiments indicated that there is a physical association between AMPK and the N-terminal cytoplasmic domain of NKCC2. Activation of AMPK in the MMDD1 (mouse macula densa-derived 1) cell line resulted in an increase in Ser126 phosphorylation in situ, suggesting that AMPK may phosphorylate NKCC2 in vivo. The functional significance of Ser126 phosphorylation was examined by mutating the serine residue to an alanine residue resulting in a marked reduction in co-transporter activity when exogenously expressed in Xenopus laevis oocytes under isotonic conditions. Under hypertonic conditions no significant change of activity was observed. Therefore the present study identifies a novel phosphorylation site that maintains NKCC2-mediated transport under isotonic or basal conditions. Moreover, the metabolic-sensing kinase, AMPK, is able to phosphorylate this site, potentially linking the cellular energy state with changes in co-transporter activity. Twit Text FOAVip Regulation of the renal-specific Na+-K+-2Cl- co-transporter NKCC2 by AMP-activated protein kinase (AMPK) ????Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=17341212 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=17341212 #FOAvip English Wikipedia <ref>{{Cite pmid|17341212}}</ref> Regulation of the renal-specific Na+-K+-2Cl- co-transporter NKCC2 by AMP-activated protein kinase (AMPK) #MMPMID17341212 Fraser SA; Gimenez I; Cook N; Jennings I; Katerelos M; Katsis F; Levidiotis V; Kemp BE; Power DA Biochem J 2007[Jul]; 405 (1): 85-93 PMID17341212show ga The renal-specific NKCC2 (Na+-K+-2Cl- co-transporter 2) is regulated by changes in phosphorylation state, however, the phosphorylation sites and kinases responsible have not been fully elucidated. In the present study, we demonstrate that the metabolic sensing kinase AMPK (AMP-activated protein kinase) phosphorylates NKCC2 on Ser126 in vitro. Co-precipitation experiments indicated that there is a physical association between AMPK and the N-terminal cytoplasmic domain of NKCC2. Activation of AMPK in the MMDD1 (mouse macula densa-derived 1) cell line resulted in an increase in Ser126 phosphorylation in situ, suggesting that AMPK may phosphorylate NKCC2 in vivo. The functional significance of Ser126 phosphorylation was examined by mutating the serine residue to an alanine residue resulting in a marked reduction in co-transporter activity when exogenously expressed in Xenopus laevis oocytes under isotonic conditions. Under hypertonic conditions no significant change of activity was observed. Therefore the present study identifies a novel phosphorylation site that maintains NKCC2-mediated transport under isotonic or basal conditions. Moreover, the metabolic-sensing kinase, AMPK, is able to phosphorylate this site, potentially linking the cellular energy state with changes in co-transporter activity. |AMP-Activated Protein Kinases[MESH] |Amino Acid Sequence[MESH] |Animals[MESH] |Antibodies, Phospho-Specific/metabolism[MESH] |Cell Line[MESH] |Enzyme Activation[MESH] |Humans[MESH] |Kidney/*metabolism[MESH] |Mice[MESH] |Molecular Sequence Data[MESH] |Multienzyme Complexes/genetics/*metabolism[MESH] |Oocytes/cytology/physiology[MESH] |Phosphorylation[MESH] |Protein Serine-Threonine Kinases/genetics/*metabolism[MESH] |Recombinant Fusion Proteins/genetics/metabolism[MESH] |Reproducibility of Results[MESH] |Rubidium/metabolism[MESH] |Sequence Alignment[MESH] |Serine/metabolism[MESH] |Sodium-Potassium-Chloride Symporters/genetics/*metabolism[MESH] |Solute Carrier Family 12, Member 1[MESH]Regulation of the renal-specific Na+-K+-2Cl- co-transporter NKCC2 by (epmc).pdf DeepDyve Pubget Overpricing