Tt. Egelhoff et al., MYOSIN-BASED CORTICAL TENSION IN DICTYOSTELIUM RESOLVED INTO HEAVY AND LIGHT CHAIN-REGULATED COMPONENTS, Journal of muscle research and cell motility, 17(2), 1996, pp. 269-274
Cortical tension in most nonmuscle cells is due largely to force produ
ction by conventional myosin (myosin II) assembled into the cytoskelet
on. Cytoskeletal contraction in smooth muscle and nonmuscle cells is i
nfluenced by the degree of myosin filament assembly, and by activation
of myosin motor function via regulatory light chain phosphorylation.
Recombinant Dictyostelium discoideum cell lines have been generated be
aring altered myosin heavy chains, resulting in either constitutive mo
tor function or constitutive assembly into the cytoskeleton. Analysis
of these cells allowed stiffening responses to agonists, measured on s
ingle cells, to be resolved into an regulatory light chain-mediated co
mponent reflecting activation of motor function, and a myosin heavy ch
ain phosphorylation-regulated component reflecting assembly of filamen
ts into the cytoskeleton. These two components can account for all of
the cortical stiffening response seen during tested in vivo contractil
e events.