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| Subject Categories: Cell & Tissue Architecture | Signal Transduction |
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| The EMBO Journal
(2006) 25, 290–301, doi:10.1038/sj.emboj.7600931 Published online 12 January 2006 |
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| TRPM7, a novel regulator of actomyosin contractility and cell adhesion |
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| Kristopher Clark1, Michiel Langeslag2, Bart van Leeuwen3, Leonie Ran3, Alexey G Ryazanov4, Carl G Figdor1, Wouter H Moolenaar3, Kees Jalink2 and Frank N van Leeuwen1 |
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1 Department of Tumor Immunology, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, Nijmegen, The Netherlands 2 Division of Cell Biology, the Netherlands Cancer Institute, Amsterdam, The Netherlands 3 Division of Cellular Biochemistry and Center for Biomedical Genetics, the Netherlands Cancer Institute, Amsterdam, The Netherlands 4 Department of Pharmacology, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ, USA To whom correspondence should be addressed Frank N van Leeuwen, Department of Tumor Immunology, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, PO Box 9101, 6500 HB Nijmegen, The Netherlands. Tel.: +31 24 361 0551; Fax: +31 24 354 0339; E-mail: f.vanleeuwen@ncmls.ru.nl Received 29 June 2005; Accepted 1 December 2005; Published online 12 January 2006. |
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| Abstract |
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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. |
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| Keywords: cell adhesion, cytoskeleton, myosin, phosphorylation, TRPM7 |
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Top of page MORE ARTICLES LIKE THISThese links to content published by NPG are automatically generated NEWS AND VIEWSNature Cell Biology News and Views (01 Sep 2008) Foot in mouth: do focal adhesions disassemble by endocytosis? Nature Cell Biology News and Views (01 Jun 2005) RESEARCHThe EMBO Journal Article (18 Oct 2006) |
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