Cargando…
Myosin light chain kinase binding to a unique site on F-actin revealed by three-dimensional image reconstruction
Ca(2+)–calmodulin-dependent phosphorylation of myosin regulatory light chains by the catalytic COOH-terminal half of myosin light chain kinase (MLCK) activates myosin II in smooth and nonmuscle cells. In addition, MLCK binds to thin filaments in situ and F-actin in vitro via a specific repeat motif...
Autores principales: | Hatch, Victoria, Zhi, Gang, Smith, Lula, Stull, James T., Craig, Roger, Lehman, William |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2001
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2196421/ https://www.ncbi.nlm.nih.gov/pubmed/11481347 http://dx.doi.org/10.1083/jcb.200105079 |
Ejemplares similares
-
Localization and Activity of Myosin Light Chain Kinase Isoforms during the Cell Cycle
por: Poperechnaya, Angela, et al.
Publicado: (2000) -
Diffusion of myosin light chain kinase on actin: A mechanism to enhance myosin phosphorylation rates in smooth muscle
por: Hong, Feng, et al.
Publicado: (2015) -
Myosin light chain kinase-driven myosin II turnover regulates actin cortex contractility during mitosis
por: Taneja, Nilay, et al.
Publicado: (2021) -
The Effects of Neuregulin on Cardiac Myosin Light Chain Kinase Gene-Ablated Hearts
por: Chang, Audrey N., et al.
Publicado: (2013) -
Myosin light chain kinase-regulated endothelial cell contraction: the relationship between isometric tension, actin polymerization, and myosin phosphorylation
Publicado: (1995)