TRPM7 Regulates Myosin IIA Filament Stability and Protein Localization by Heavy Chain Phosphorylation

Deregulation of myosin II-based contractility contributes to the pathogenesis of human diseases, such as cancer, which underscores the necessity for tight spatial and temporal control of myosin II activity. Recently, we demonstrated that activation of the mammalian α-kinase TRPM7 inhibits myosin II-...

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Veröffentlicht in:	Journal of molecular biology 2008-05, Vol.378 (4), p.790-803
Hauptverfasser:	Clark, Kristopher, Middelbeek, Jeroen, Lasonder, Edwin, Dulyaninova, Natalya G., Morrice, Nick A., Ryazanov, Alexey G., Bresnick, Anne R., Figdor, Carl G., van Leeuwen, Frank N.
Format:	Artikel
Sprache:	eng
Schlagworte:	actin Amino Acid Sequence Animals Cell Line Cercopithecus aethiops Conserved Sequence cytoskeleton Humans Kinetics Mice Molecular Sequence Data Mutation - genetics Myosin Heavy Chains - metabolism myosin IIA Nonmuscle Myosin Type IIA - chemistry Nonmuscle Myosin Type IIA - genetics Nonmuscle Myosin Type IIA - metabolism Phosphorylation Phosphoserine - metabolism Phosphothreonine - metabolism Sequence Alignment TRPM Cation Channels - genetics TRPM Cation Channels - metabolism TRPM7
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