Abstract
Phosphorylation of myosin light chain kinase by a Ca2+-dependent protein kinase increases the concentration of Ca2+/calmodulin required for half-maximal activation. The Ca2+ concentrations required for myosin light chain kinase phosphorylation in permeable smooth muscle are similar to those required for myosin light chain phosphorylation. Both GTPγS and carbachol increase the Ca2+ sensitivity of myosin light chain kinase phosphorylation as well as light chain phosphorylation. It is proposed that a similar G-protein mediated mechanism regulates the Ca2+-dependent phosphorylation of these two contractile proteins in smooth muscle.
Original language | English (US) |
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Pages (from-to) | 272-275 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 331 |
Issue number | 3 |
DOIs | |
State | Published - Oct 4 1993 |
Keywords
- GTPγS
- Myosin light chain
- Myosin light chain kinase
- Protein phosphatase
- Smooth muscle contraction
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology