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10.1042/BJ20081405 http://scihub22266oqcxt.onion/10.1042/BJ20081405 19228120!ä!19228120 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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\19228120.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biochem+J 2009 ; 420 (1): 115-22 Nephropedia Template TP {{tp|p=19228120|t=2009. Identification of dimer interactions required for the catalytic activity of the TRPM7 alpha-kinase domain |pdf=|usr=}}{{19228120}} gab.com Text Identification of dimer interactions required for the catalytic activity of the TRPM7 alpha-kinase domain JO: Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=19228120 #FOAvip TRPM7 (transient receptor potential melastatin) combines an ion channel domain with a C-terminal protein kinase domain that belongs to the atypical alpha-kinase family. The TRPM7 alpha-kinase domain assembles into a dimer through the exchange of an N-terminal segment that extends from residue 1551 to residue 1577 [Yamaguchi, Matsushita, Nairn and Kuriyan (2001) Mol. Cell 7, 1047-1057]. Here, we show, by analysis of truncation mutants, that residues 1553-1562 of the N-terminus are essential for kinase activity but not dimer formation. Within this 'activation sequence', site-directed mutagenesis identified Tyr-1553 and Arg-1558 as residues critical for activity. Examination of the TRPM7 kinase domain structure suggests that the activation sequence interacts with the other subunit to help position a catalytic loop that contains the invariant Asp-1765 residue. Residues 1563-1570 of the N-terminal segment are critical for dimer assembly. Mutation of Leu-1564, Ile-1568 or Phe-1570 to alanine abolished both kinase activity and dimer formation. The activity of a monomeric TRPM7 kinase domain lacking the entire N-terminal segment was rescued by a GST (glutathione transferase) fusion protein containing residues 1548-1576 of TRPM7, showing that all interactions essential for activity are provided by the N-terminal segment. Activity was also restored by GST fused to the N-terminal segment of TRPM6 (residues 1711-1740), demonstrating the feasibility of forming functional TRPM6-TRPM7 alpha-kinase domain heterodimers. It is proposed that covalent modifications or binding interactions that alter the conformation of the N-terminal exchanged segment may provide a means to regulate TRPM7 kinase activity. Twit Text FOAVip Identification of dimer interactions required for the catalytic activity of the TRPM7 alpha-kinase domain ????Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=19228120 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=19228120 #FOAvip English Wikipedia <ref>{{Cite pmid|19228120}}</ref> Identification of dimer interactions required for the catalytic activity of the TRPM7 alpha-kinase domain #MMPMID19228120 Crawley SW; Cote GP Biochem J 2009[Apr]; 420 (1): 115-22 PMID19228120show ga TRPM7 (transient receptor potential melastatin) combines an ion channel domain with a C-terminal protein kinase domain that belongs to the atypical alpha-kinase family. The TRPM7 alpha-kinase domain assembles into a dimer through the exchange of an N-terminal segment that extends from residue 1551 to residue 1577 [Yamaguchi, Matsushita, Nairn and Kuriyan (2001) Mol. Cell 7, 1047-1057]. Here, we show, by analysis of truncation mutants, that residues 1553-1562 of the N-terminus are essential for kinase activity but not dimer formation. Within this 'activation sequence', site-directed mutagenesis identified Tyr-1553 and Arg-1558 as residues critical for activity. Examination of the TRPM7 kinase domain structure suggests that the activation sequence interacts with the other subunit to help position a catalytic loop that contains the invariant Asp-1765 residue. Residues 1563-1570 of the N-terminal segment are critical for dimer assembly. Mutation of Leu-1564, Ile-1568 or Phe-1570 to alanine abolished both kinase activity and dimer formation. The activity of a monomeric TRPM7 kinase domain lacking the entire N-terminal segment was rescued by a GST (glutathione transferase) fusion protein containing residues 1548-1576 of TRPM7, showing that all interactions essential for activity are provided by the N-terminal segment. Activity was also restored by GST fused to the N-terminal segment of TRPM6 (residues 1711-1740), demonstrating the feasibility of forming functional TRPM6-TRPM7 alpha-kinase domain heterodimers. It is proposed that covalent modifications or binding interactions that alter the conformation of the N-terminal exchanged segment may provide a means to regulate TRPM7 kinase activity. |Amino Acid Sequence[MESH] |Animals[MESH] |Catalysis[MESH] |Mice[MESH] |Protein Kinases/metabolism[MESH] |Protein Multimerization[MESH] |Protein Structure, Tertiary[MESH] |Protein Subunits[MESH]Identification of dimer interactions required for the catalytic activi(epmc).pdf DeepDyve Pubget Overpricing