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10.1042/BJ20101678 http://scihub22266oqcxt.onion/10.1042/BJ20101678 C3507444!3507444!21208190     free     free     free       Biochem+J 2011 ; 434 (3): 513-21 Nephropedia Template TP {{tp|p=21208190|t=2011. TRPM7 Regulates Polarized Cell Movements |pdf=|usr=}}{{21208190}} gab.com Text TRPM7 Regulates Polarized Cell Movements JO: Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=21208190 #FOAvip TRPM7 is a Ca2+ and Mg2+ permeant ion channel in possession of its own kinase domain. As a kinase, the protein has been linked to the control of actomyosin contractility, whereas the channel has been found to regulate cell adhesion as well as cellular Mg2+ homeostasis. Here we show that depletion of TRPM7 by RNA interference in fibroblasts alters cell morphology, the cytoskeleton, and the ability of cells to form lamellipodia and to execute polarized cell movements. A pulldown purification assay revealed that knockdown of TRPM7 prevents cells from activating Rac and Cdc42 when stimulated to migrate into a cellular wound. Re-expression of TRPM7 reverses these phenotypic changes, as does, unexpectedly, expression of a kinase-inactive mutant of TRPM7. Surprisingly, expression of the Mg2+ transporter SLC41A2 is also effective restoring the change in cell morphology, disruption of the cytoskeleton, and directional cell motility caused by depletion of the channel-kinase. These data uncover an essential role for Mg2+ in TRPM7's control over the cytoskeleton and its ability to regulate polarized cell movements. Twit Text FOAVip TRPM7 Regulates Polarized Cell Movements ????Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=21208190 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=21208190 #FOAvip English Wikipedia <ref>{{Cite pmid|21208190}}</ref> TRPM7 Regulates Polarized Cell Movements #MMPMID21208190 Su LT; Liu W; Chen HC; González-Pagán O; Habas R; Runnels LW Biochem J 2011[Mar]; 434 (3): 513-21 PMID21208190show ga TRPM7 is a Ca2+ and Mg2+ permeant ion channel in possession of its own kinase domain. As a kinase, the protein has been linked to the control of actomyosin contractility, whereas the channel has been found to regulate cell adhesion as well as cellular Mg2+ homeostasis. Here we show that depletion of TRPM7 by RNA interference in fibroblasts alters cell morphology, the cytoskeleton, and the ability of cells to form lamellipodia and to execute polarized cell movements. A pulldown purification assay revealed that knockdown of TRPM7 prevents cells from activating Rac and Cdc42 when stimulated to migrate into a cellular wound. Re-expression of TRPM7 reverses these phenotypic changes, as does, unexpectedly, expression of a kinase-inactive mutant of TRPM7. Surprisingly, expression of the Mg2+ transporter SLC41A2 is also effective restoring the change in cell morphology, disruption of the cytoskeleton, and directional cell motility caused by depletion of the channel-kinase. These data uncover an essential role for Mg2+ in TRPM7's control over the cytoskeleton and its ability to regulate polarized cell movements. äTRPM7 Regulates Polarized Cell Movements (epmc).pdf DeepDyve Pubget Overpricing