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A more recent version of this article appeared on April 21, 2006 Originally published In Press as doi:10.1074/jbc.M512885200 on January 31, 2006
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Papers In Press, published online ahead of print January 25, 2006
J. Biol. Chem, 10.1074/jbc.M512885200
Submitted on December 2, 2005
Revised on January 23, 2006
Accepted on January 25, 2006

Trpm7 regulates cell adhesion by controlling the calcium dependent protease calpain

Li-Ting Su, Maria A. Agapito, Mingjiang Li, Will Simpson, Anna Huttenlocher, Raymond Habas, Lixia Yue, and Loren W. Runnels

Pharmacolgy Dept., UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ 08854

Corresponding Author: runnellw{at}umdnj.edu

M-calpain is a protease implicated in the control of cell adhesion through focal adhesion disassembly. The mechanism by which the enzyme is spatially and temporally controlled is not well understood, particularly because calpain’s dependence on calcium exceeds the sub-micromolar concentrations normally observed in cells. Here we show that the channel-kinase TRPM7 localizes to peripheral adhesion complexes with m-calpain, where it regulates cell adhesion by controlling the activity of the protease. Our research revealed that overexpression of TRPM7 in cells caused cell rounding with a concomitant loss of cell adhesion that is dependent upon the protein’s channel but not its kinase activities. Knockdown of m-calpain blocked TRPM7-induced cell rounding and cell detachment. Silencing of TRPM7 by RNA interference, however, strengthened cell adhesion and increased the number of peripheral adhesion complexes in the cells. Together, our results suggest that the ion channel TRPM7 regulates cell adhesion through m-calpain by mediating local influx of calcium into peripheral adhesion complexes.


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