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10.1074/jbc.M113.512285 http://scihub22266oqcxt.onion/10.1074/jbc.M113.512285 24385424!3931078!24385424     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24385424&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       J+Biol+Chem 2014 ; 289 (8): 5217-27 Nephropedia Template TP {{tp|p=24385424|t=2014. The TRPM6 kinase domain determines the Mg ATP sensitivity of TRPM7/M6 heteromeric ion channels |pdf=|usr=}}{{24385424}} gab.com Text The TRPM6 kinase domain determines the Mg ATP sensitivity of TRPM7/M6 heteromeric ion channels JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=24385424 #FOAvip The transient receptor potential melastatin member 7 (TRPM7) and member 6 (TRPM6) are divalent cation channel kinases essential for magnesium (Mg(2+)) homeostasis in vertebrates. It remains unclear how TRPM6 affects divalent cation transport and whether this involves functional homomeric TRPM6 plasma membrane channels or heteromeric channel assemblies with TRPM7. We show that homomeric TRPM6 is highly sensitive to intracellular free Mg(2+) and therefore unlikely to be active at physiological levels of [Mg(2+)]i. Co-expression of TRPM7 and TRPM6 produces heteromeric TRPM7/M6 channels with altered pharmacology and sensitivity to intracellular Mg.ATP compared with homomeric TRPM7. Strikingly, the activity of heteromeric TRPM7/M6 channels is independent of intracellular Mg.ATP concentrations, essentially uncoupling channel activity from cellular energy status. Disruption of TRPM6 kinase phosphorylation activity re-introduces Mg.ATP sensitivity to the heteromeric channel similar to that of TRPM7. Thus, TRPM6 modulates the functionality of TRPM7, and the TRPM6 kinase plays a critical role in tuning the phenotype of the TRPM7.M6 channel complex. Twit Text FOAVip The TRPM6 kinase domain determines the Mg ATP sensitivity of TRPM7/M6 heteromeric ion channels ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=24385424 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24385424 #FOAvip English Wikipedia <ref>{{Cite pmid|24385424}}</ref> The TRPM6 kinase domain determines the Mg ATP sensitivity of TRPM7/M6 heteromeric ion channels #MMPMID24385424 Zhang Z; Yu H; Huang J; Faouzi M; Schmitz C; Penner R; Fleig A J Biol Chem 2014[Feb]; 289 (8): 5217-27 PMID24385424show ga The transient receptor potential melastatin member 7 (TRPM7) and member 6 (TRPM6) are divalent cation channel kinases essential for magnesium (Mg(2+)) homeostasis in vertebrates. It remains unclear how TRPM6 affects divalent cation transport and whether this involves functional homomeric TRPM6 plasma membrane channels or heteromeric channel assemblies with TRPM7. We show that homomeric TRPM6 is highly sensitive to intracellular free Mg(2+) and therefore unlikely to be active at physiological levels of [Mg(2+)]i. Co-expression of TRPM7 and TRPM6 produces heteromeric TRPM7/M6 channels with altered pharmacology and sensitivity to intracellular Mg.ATP compared with homomeric TRPM7. Strikingly, the activity of heteromeric TRPM7/M6 channels is independent of intracellular Mg.ATP concentrations, essentially uncoupling channel activity from cellular energy status. Disruption of TRPM6 kinase phosphorylation activity re-introduces Mg.ATP sensitivity to the heteromeric channel similar to that of TRPM7. Thus, TRPM6 modulates the functionality of TRPM7, and the TRPM6 kinase plays a critical role in tuning the phenotype of the TRPM7.M6 channel complex. |Adenosine Triphosphate/*pharmacology[MESH] |Boron Compounds/pharmacology[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Intracellular Space/drug effects/metabolism[MESH] |Ion Channel Gating/drug effects[MESH] |Osmolar Concentration[MESH] |Phosphotransferases/metabolism[MESH] |Point Mutation/genetics[MESH] |Protein Serine-Threonine Kinases[MESH] |Protein Structure, Tertiary[MESH] |Solutions[MESH] |Structure-Activity Relationship[MESH]The TRPM6 kinase domain determines the Mg ATP sensitivity of TRPM7/M6 (epmc).pdf DeepDyve Pubget Overpricing