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10.1074/jbc.RA118.004066 http://scihub22266oqcxt.onion/10.1074/jbc.RA118.004066 30305398!6254349!30305398     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=30305398&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 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 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 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 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 2018 ; 293 (47): 18151-18167 Nephropedia Template TP {{tp|p=30305398|t=2018. Depletion of plasma membrane-associated phosphoinositides mimics inhibition of TRPM7 channels by cytosolic Mg(2+), spermine, and pH |pdf=|usr=}}{{30305398}} gab.com Text Depletion of plasma membrane-associated phosphoinositides mimics inhibition of TRPM7 channels by cytosolic Mg(2+), spermine, and pH JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=30305398 #FOAvip Transient receptor potential cation channel subfamily M member 7 (TRPM7) is an ion channel/protein kinase belonging to the TRP melastatin and eEF2 kinase families. Under physiological conditions, most native TRPM7 channels are inhibited by cytoplasmic Mg(2+), protons, and polyamines. Currents through these channels (I(TRPM7)) are robustly potentiated when the cell interior is exchanged with low Mg(2+)-containing buffers. I(TRPM7) is also potentiated by phosphatidyl inositol bisphosphate (PI(4,5)P(2)) and suppressed by its hydrolysis. Here we characterized internal Mg(2+)- and pH-mediated inhibition of TRPM7 channels in HEK293 cells overexpressing WT voltage-sensing phospholipid phosphatase (VSP) or its catalytically inactive variant VSP-C363S. VSP-mediated depletion of membrane phosphoinositides significantly increased channel sensitivity to Mg(2+) and pH. Proton concentrations that were too low to inhibit I(TRPM7) when the VSP-C363S variant was expressed (pH 8.2) became inhibitory in WT VSP-expressing cells. At pH 6.5, protons inhibited I(TRPM7) both in WT and VSP C363S-expressing cells but with a faster time course in the WT VSP-expressing cells. Inhibition by 150 mum Mg(2+) was also significantly faster in the WT VSP-expressing cells. Cellular PI(4,5)P(2) depletion increased the sensitivity of TRPM7 channels to the inhibitor 2-aminoethyl diphenyl borinate, which acidifies the cytosol. Single substitutions at Ser-1107 of TRPM7, reducing its sensitivity to Mg(2+), also decreased its inhibition by spermine and acidic pH. Furthermore, these channel variants were markedly less sensitive to VSP-mediated PI(4,5)P(2) depletion than the WT. We conclude that the internal Mg(2+)-, polyamine-, and pH-mediated inhibition of TRPM7 channels is not direct but, rather, reflects electrostatic screening and resultant disruption of PI(4,5)P(2)-channel interactions. Twit Text FOAVip Depletion of plasma membrane-associated phosphoinositides mimics inhibition of TRPM7 channels by cytosolic Mg(2+), spermine, and pH ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=30305398 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=30305398 #FOAvip English Wikipedia <ref>{{Cite pmid|30305398}}</ref> Depletion of plasma membrane-associated phosphoinositides mimics inhibition of TRPM7 channels by cytosolic Mg(2+), spermine, and pH #MMPMID30305398 Zhelay T; Wieczerzak KB; Beesetty P; Alter GM; Matsushita M; Kozak JA J Biol Chem 2018[Nov]; 293 (47): 18151-18167 PMID30305398show ga Transient receptor potential cation channel subfamily M member 7 (TRPM7) is an ion channel/protein kinase belonging to the TRP melastatin and eEF2 kinase families. Under physiological conditions, most native TRPM7 channels are inhibited by cytoplasmic Mg(2+), protons, and polyamines. Currents through these channels (I(TRPM7)) are robustly potentiated when the cell interior is exchanged with low Mg(2+)-containing buffers. I(TRPM7) is also potentiated by phosphatidyl inositol bisphosphate (PI(4,5)P(2)) and suppressed by its hydrolysis. Here we characterized internal Mg(2+)- and pH-mediated inhibition of TRPM7 channels in HEK293 cells overexpressing WT voltage-sensing phospholipid phosphatase (VSP) or its catalytically inactive variant VSP-C363S. VSP-mediated depletion of membrane phosphoinositides significantly increased channel sensitivity to Mg(2+) and pH. Proton concentrations that were too low to inhibit I(TRPM7) when the VSP-C363S variant was expressed (pH 8.2) became inhibitory in WT VSP-expressing cells. At pH 6.5, protons inhibited I(TRPM7) both in WT and VSP C363S-expressing cells but with a faster time course in the WT VSP-expressing cells. Inhibition by 150 mum Mg(2+) was also significantly faster in the WT VSP-expressing cells. Cellular PI(4,5)P(2) depletion increased the sensitivity of TRPM7 channels to the inhibitor 2-aminoethyl diphenyl borinate, which acidifies the cytosol. Single substitutions at Ser-1107 of TRPM7, reducing its sensitivity to Mg(2+), also decreased its inhibition by spermine and acidic pH. Furthermore, these channel variants were markedly less sensitive to VSP-mediated PI(4,5)P(2) depletion than the WT. We conclude that the internal Mg(2+)-, polyamine-, and pH-mediated inhibition of TRPM7 channels is not direct but, rather, reflects electrostatic screening and resultant disruption of PI(4,5)P(2)-channel interactions. |Animals[MESH] |Biological Transport[MESH] |Cell Membrane/genetics/*metabolism[MESH] |Cytosol/*metabolism[MESH] |Hydrogen-Ion Concentration[MESH] |Magnesium/*metabolism[MESH] |Mice[MESH] |Patch-Clamp Techniques[MESH] |Phosphatidylinositol 4,5-Diphosphate/metabolism[MESH] |Phosphatidylinositols/*metabolism[MESH] |Polyamines/metabolism[MESH] |Protons[MESH] |Spermine/*metabolism[MESH]Depletion of plasma membrane-associated phosphoinositides mimics inhib(epmc).pdf DeepDyve Pubget Overpricing