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J Physiol Volume 516, Number 3, 630-, May 1, 1999
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The Journal of Physiology (1999), 516.3, p. 630
© Copyright 1999 The Physiological Society

Kinases, myosin phosphatase and Rho proteins: curiouser and curiouser

Andrew P. Somlyo

Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22906-0011, USA

The primary mechanism activating smooth muscle is phosphorylation of the myosin regulatory light chain (MLC20) by a myosin light chain kinase (MLCK) activated by Ca2+- calmodulin (CaM)-dependent phosphorylation; this allows actin to activate myosin ATPase, causing muscle to contract. Inactivation (relaxation) occurs as the result of dephosphorylation of MLC20 by a heterotrimeric smooth muscle myosin phosphatase, SMPP-1M (Hartshorne et al. 1998). Dephosphorylation of MLC20 was thought to be by an unregulated 'housekeeping' enzyme, until it was recognized that it can be regulated, independently of changes in [Ca2+]i, by G-protein-coupled cascades (Somlyo et al. 1989). These and related (Gallagher et al. 1997) signal transduction mechanisms play physiologically important roles in both smooth muscles and in non-muscle cells in which cytoplasmic myosin II motors are regulated by phosphorylation/dephosphorylation (Somlyo & Somlyo, 1994). Two proteins involved in such mechanisms are reported in this issue of The Journal of Physiology .


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