Dephosphorylation of the two regulatory components of myosin phosphatase, MBS and CPI17
Open Access
- 5 March 2002
- journal article
- Published by Wiley in FEBS Letters
- Vol. 515 (1-3) , 127-132
- https://doi.org/10.1016/s0014-5793(02)02451-1
Abstract
Dephosphorylation of the two key regulatory factors of myosin light chain phosphatase (MLCP), CPI17 and MBS (myosin binding subunit) of MLCP was studied. While Thr38 phosphorylated CPI17 is quite sus...Keywords
This publication has 40 references indexed in Scilit:
- Signal transduction by G‐proteins, Rho‐kinase and protein phosphatase to smooth muscle and non‐muscle myosin IIThe Journal of Physiology, 2000
- Inhibitory Phosphorylation Site for Rho-associated Kinase on Smooth Muscle Myosin PhosphataseJournal of Biological Chemistry, 1999
- ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cellsFEBS Letters, 1999
- Phosphorylation and Activation of Myosin by Rho-associated Kinase (Rho-kinase)Journal of Biological Chemistry, 1996
- Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase)Science, 1996
- Phosphorylation by MAPKAP Kinase 2 Activates Mg2+-ATPase Activity of Myosin IIBiochemical and Biophysical Research Communications, 1996
- The control of protein phosphatase‐1 by targetting subunitsEuropean Journal of Biochemistry, 1992
- CONTROL OF NONMUSCLE MYOSINS BY PHOSPHORYLATIONAnnual Review of Biochemistry, 1992
- Regulation of cytoplasmic and smooth muscle myosinCurrent Opinion in Cell Biology, 1991
- Regulation of Smooth Muscle Contractile Elements by Second MessengersAnnual Review of Physiology, 1989