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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.
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Biochem+J 2011 ; 434 (3): 513-21
