Department of Cell Biology; Department of Physiology
Actins; Adenosine Triphosphatases; Animals; *Gene Expression Regulation; Image Processing, Computer-Assisted; Microscopy, Electron; Models, Biological; Molecular Conformation; Muscle, Skeletal; Myosin Heavy Chains; Myosins; Pectinidae; Phosphorylation; Protein Binding; Protein Structure, Tertiary
Life Sciences | Medicine and Health Sciences
Intramolecular interaction between myosin heads, blocking key sites involved in actin-binding and ATPase activity, appears to be a critical mechanism for switching off vertebrate smooth-muscle myosin molecules, leading to relaxation. We have tested the hypothesis that this interaction is a general mechanism for switching off myosin II-based motile activity in both muscle and nonmuscle cells. Electron microscopic images of negatively stained myosin II molecules were analyzed by single particle image processing. Molecules from invertebrate striated muscles with phosphorylation-dependent regulation showed head-head interactions in the off-state similar to those in vertebrate smooth muscle. A similar structure was observed in nonmuscle myosin II (also phosphorylation-regulated). Surprisingly, myosins from vertebrate skeletal and cardiac muscle, which are not intrinsically regulated, undergo similar head-head interactions in relaxing conditions. In all of these myosins, we also observe conserved interactions between the 'blocked' myosin head and the myosin tail, which may contribute to the switched-off state. These results suggest that intramolecular head-head and head-tail interactions are a general mechanism both for inducing muscle relaxation and for switching off myosin II-based motile activity in nonmuscle cells. These interactions are broken when myosin is activated.
DOI of Published Version
Mol Biol Cell. 2008 Aug;19(8):3234-42. Epub 2008 May 21. Link to article on publisher's site
Molecular biology of the cell
Jung H, Komatsu S, Ikebe M, Craig RW. (2008). Head-head and head-tail interaction: a general mechanism for switching off myosin II activity in cells. Open Access Publications by UMMS Authors. https://doi.org/10.1091/mbc.E08-02-0206. Retrieved from https://escholarship.umassmed.edu/oapubs/1958