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10.1038/sj.emboj.7600931 http://scihub22266oqcxt.onion/10.1038/sj.emboj.7600931 C1383514!1383514!16407977     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       EMBO+J 2006 ; 25 (2): 290-301 Nephropedia Template TP {{tp|p=16407977|t=2006. TRPM7, a novel regulator of actomyosin contractility and cell adhesion |pdf=|usr=}}{{16407977}} gab.com Text TRPM7, a novel regulator of actomyosin contractility and cell adhesion JO: EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=16407977 #FOAvip Actomyosin contractility regulates various cell biological processes including cytokinesis, adhesion and migration. While in lower eukaryotes, ?-kinases control actomyosin relaxation, a similar role for mammalian ?-kinases has yet to be established. Here, we examined whether TRPM7, a cation channel fused to an ?-kinase, can affect actomyosin function. We demonstrate that activation of TRPM7 by bradykinin leads to a Ca2+- and kinase-dependent interaction with the actomyosin cytoskeleton. Moreover, TRPM7 phosphorylates the myosin IIA heavy chain. Accordingly, low overexpression of TRPM7 increases intracellular Ca2+ levels accompanied by cell spreading, adhesion and the formation of focal adhesions. Activation of TRPM7 induces the transformation of these focal adhesions into podosomes by a kinase-dependent mechanism, an effect that can be mimicked by pharmacological inhibition of myosin II. Collectively, our results demonstrate that regulation of cell adhesion by TRPM7 is the combined effect of kinase-dependent and -independent pathways on actomyosin contractility. Twit Text FOAVip TRPM7, a novel regulator of actomyosin contractility and cell adhesion ????EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=16407977 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=16407977 #FOAvip English Wikipedia <ref>{{Cite pmid|16407977}}</ref> TRPM7, a novel regulator of actomyosin contractility and cell adhesion #MMPMID16407977 Clark K; Langeslag M; van Leeuwen B; Ran L; Ryazanov AG; Figdor CG; Moolenaar WH; Jalink K; van Leeuwen FN EMBO J 2006[Jan]; 25 (2): 290-301 PMID16407977show ga Actomyosin contractility regulates various cell biological processes including cytokinesis, adhesion and migration. While in lower eukaryotes, ?-kinases control actomyosin relaxation, a similar role for mammalian ?-kinases has yet to be established. Here, we examined whether TRPM7, a cation channel fused to an ?-kinase, can affect actomyosin function. We demonstrate that activation of TRPM7 by bradykinin leads to a Ca2+- and kinase-dependent interaction with the actomyosin cytoskeleton. Moreover, TRPM7 phosphorylates the myosin IIA heavy chain. Accordingly, low overexpression of TRPM7 increases intracellular Ca2+ levels accompanied by cell spreading, adhesion and the formation of focal adhesions. Activation of TRPM7 induces the transformation of these focal adhesions into podosomes by a kinase-dependent mechanism, an effect that can be mimicked by pharmacological inhibition of myosin II. Collectively, our results demonstrate that regulation of cell adhesion by TRPM7 is the combined effect of kinase-dependent and -independent pathways on actomyosin contractility. äTRPM7, a novel regulator of actomyosin contractility and cell adhesion(epmc).pdf DeepDyve Pubget Overpricing