Regulation of the function of mammalian myosin and its conformational change.
It has been known that the phosphorylation of the regulatory light chain, residing at the head/rod junction of the molecule activates the motor activity of smooth muscle and non-muscle conventional myosin (myosin II), and triggers a large conformational change of the molecule from the inhibited folded conformation to the active extended conformation. Recent structural analysis has revealed the structural basis of the inhibition of the motor function of the two heads in the inhibited conformation. On the other hand, recent studies have revealed that a processive unconventional myosin, myosin V, also shows a large change in the conformation from the folded to an extended form and this explains the activation mechanism of myosin V motor activity. These findings suggest the presence of a common scenario for the regulation of motor protein functions.
Ikebe
Mitsuo
M
Department of Physiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA.
D001665:Binding Sites; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D009038:Motion; D024462:Myosin Type II / Q000737:chemistry* / Q000648:ultrastructure*; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D020409:Molecular Motor Proteins; D024462:Myosin Type II