Involvement of Tail Domains in Regulation of Dictyostelium Myosin II
- 1 April 2000
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 271 (1), 75-81
- https://doi.org/10.1006/bbrc.2000.2582
Abstract
No abstract availableThis publication has 40 references indexed in Scilit:
- The Interaction between the Regulatory Light Chain Domains on Two Heads Is Critical for Regulation of Smooth Muscle MyosinBiochemistry, 2000
- Filament structure as an essential factor for regulation of Dictyostelium myosin by regulatory light chain phosphorylationProceedings of the National Academy of Sciences, 1998
- Spare the rod, spoil the regulation: Necessity for a myosin rodProceedings of the National Academy of Sciences, 1997
- Expression of a myosin regulatory light chain phosphorylation site mutant complements the cytokinesis and developmental defects of Dictyostelium RMLC null cells.The Journal of cell biology, 1994
- Regulation of Dictyostelium myosin II by phosphorylation: what is essential and what is important?The Journal of cell biology, 1994
- A Dictyostelium myosin II lacking a proximal 58-kDa portion of the tail is functional in vitro and in vivo.Molecular Biology of the Cell, 1992
- CONTROL OF NONMUSCLE MYOSINS BY PHOSPHORYLATIONAnnual Review of Biochemistry, 1992
- Effect of heavy chain phosphorylation on the polymerization and structure of Dictyostelium myosin filaments.The Journal of cell biology, 1987
- Myosin light chain kinase and myosin light chain phosphatase from Dictyostelium: effects of reversible phosphorylation on myosin structure and function.The Journal of cell biology, 1987
- Proteolysis of smooth muscle myosin by Staphylococcus aureus protease: preparation of heavy meromyosin and subfragment 1 with intact 20,000-dalton light chainsBiochemistry, 1985