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TRPM7, a novel regulator of actomyosin contractility and cell adhesion
Author(s) -
Clark Kristopher,
Langeslag Michiel,
van Leeuwen Bart,
Ran Leonie,
Ryazanov Alexey G,
Figdor Carl G,
Moolenaar Wouter H,
Jalink Kees,
van Leeuwen Frank N
Publication year - 2006
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600931
Subject(s) - biology , regulator , contractility , microbiology and biotechnology , adhesion , cell adhesion , biophysics , cell , biochemistry , endocrinology , gene , chemistry , organic chemistry
Actomyosin contractility regulates various cell biological processes including cytokinesis, adhesion and migration. While in lower eukaryotes, α‐kinases control actomyosin relaxation, a similar role for mammalian α‐kinases has yet to be established. Here, we examined whether TRPM7, a cation channel fused to an α‐kinase, can affect actomyosin function. We demonstrate that activation of TRPM7 by bradykinin leads to a Ca 2+ ‐ and kinase‐dependent interaction with the actomyosin cytoskeleton. Moreover, TRPM7 phosphorylates the myosin IIA heavy chain. Accordingly, low overexpression of TRPM7 increases intracellular Ca 2+ 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.