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10.1074/jbc.M800167200 http://scihub22266oqcxt.onion/10.1074/jbc.M800167200 18490453!ä!18490453 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2008 ; 283 (29): 19999-20007 Nephropedia Template TP {{tp|p=18490453|t=2008. Role of the alpha-kinase domain in transient receptor potential melastatin 6 channel and regulation by intracellular ATP |pdf=|usr=}}{{18490453}} gab.com Text Role of the alpha-kinase domain in transient receptor potential melastatin 6 channel and regulation by intracellular ATP JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=18490453 #FOAvip Transient receptor potential melastatin 6 (TRPM6) plays an essential role in epithelial Mg(2+) transport. TRPM6 and its closest homologue, TRPM7, both combine a cation channel with an alpha-kinase domain. However, the role of this alpha-kinase domain in TRPM6 channel activity remains elusive. The aim of this study was to investigate the regulation of TRPM6 channel activity by intracellular ATP and the involvement of its alpha-kinase domain. We demonstrated that intracellular Na- and Mg-ATP decreased the TRPM6 current in HEK293 cells heterogeneously expressing the channel, whereas Na-CTP or Na-GTP had no effect on channel activity. Whole cell recordings in TRPM6-expressing HEK293 cells showed that deletion of the alpha-kinase domain prevented the inhibitory effect of intracellular ATP without abrogating channel activity. Mutation of the conserved putative ATP-binding motif GXG(A)XXG (G1955D) in the alpha-kinase domain of TRPM6 inhibited the ATP action, whereas this effect remained preserved in the TRPM6 phosphotransferase-deficient mutant K1804R. Mutation of the TRPM6 autophosphorylation site, Thr(1851), into either an alanine or an aspartate, resulted in functional channels that could still be inhibited by ATP. In conclusion, intracellular ATP regulates TRPM6 channel activity via its alpha-kinase domain independently of alpha-kinase activity. Twit Text FOAVip Role of the alpha-kinase domain in transient receptor potential melastatin 6 channel and regulation by intracellular ATP ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=18490453 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=18490453 #FOAvip English Wikipedia <ref>{{Cite pmid|18490453}}</ref> Role of the alpha-kinase domain in transient receptor potential melastatin 6 channel and regulation by intracellular ATP #MMPMID18490453 Thebault S; Cao G; Venselaar H; Xi Q; Bindels RJ; Hoenderop JG J Biol Chem 2008[Jul]; 283 (29): 19999-20007 PMID18490453show ga Transient receptor potential melastatin 6 (TRPM6) plays an essential role in epithelial Mg(2+) transport. TRPM6 and its closest homologue, TRPM7, both combine a cation channel with an alpha-kinase domain. However, the role of this alpha-kinase domain in TRPM6 channel activity remains elusive. The aim of this study was to investigate the regulation of TRPM6 channel activity by intracellular ATP and the involvement of its alpha-kinase domain. We demonstrated that intracellular Na- and Mg-ATP decreased the TRPM6 current in HEK293 cells heterogeneously expressing the channel, whereas Na-CTP or Na-GTP had no effect on channel activity. Whole cell recordings in TRPM6-expressing HEK293 cells showed that deletion of the alpha-kinase domain prevented the inhibitory effect of intracellular ATP without abrogating channel activity. Mutation of the conserved putative ATP-binding motif GXG(A)XXG (G1955D) in the alpha-kinase domain of TRPM6 inhibited the ATP action, whereas this effect remained preserved in the TRPM6 phosphotransferase-deficient mutant K1804R. Mutation of the TRPM6 autophosphorylation site, Thr(1851), into either an alanine or an aspartate, resulted in functional channels that could still be inhibited by ATP. In conclusion, intracellular ATP regulates TRPM6 channel activity via its alpha-kinase domain independently of alpha-kinase activity. |Adenosine Triphosphate/*metabolism[MESH] |Amino Acid Motifs[MESH] |Amino Acid Sequence[MESH] |Cell Line[MESH] |Electrophysiology[MESH] |Humans[MESH] |Models, Molecular[MESH] |Molecular Sequence Data[MESH] |Mutation/genetics[MESH] |Patch-Clamp Techniques[MESH] |Protein Kinases/chemistry/genetics/*metabolism[MESH] |Protein Structure, Tertiary[MESH] |Substrate Specificity[MESH]Role of the alpha-kinase domain in transient receptor potential melast(epmc).pdf DeepDyve Pubget Overpricing