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2011 ; 434
(3
): 513-21
Nephropedia Template TP
Su LT
; Liu W
; Chen HC
; González-Pagán O
; Habas R
; Runnels LW
Biochem J
2011[Mar]; 434
(3
): 513-21
PMID21208190
show ga
TRPM7 (transient receptor potential melastatin 7) 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+ homoeostasis. In
the present study 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 (cell division cycle 42) 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 (solute carrier family
41 member 2) is also effective in restoring the change in cell morphology,
disruption of the cytoskeleton and directional cell motility caused by depletion
of the channel-kinase. The results of the present study uncover an essential role
for Mg²+ in the control of TRPM7 over the cytoskeleton and its ability to
regulate polarized cell movements.
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