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Vol. 10, Issue 10, 3097-3112, October 1999
*Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
11724; and Departments of Caldesmon is known to inhibit the ATPase activity of actomyosin in
a Ca2+-calmodulin-regulated manner. Although a nonmuscle
isoform of caldesmon is widely expressed, its functional role has not
yet been elucidated. We studied the effects of nonmuscle caldesmon on
cellular contractility, actin cytoskeletal organization, and the
formation of focal adhesions in fibroblasts. Transient transfection of
nonmuscle caldesmon prevents myosin II-dependent cell contractility and
induces a decrease in the number and size of tyrosine-phosphorylated focal adhesions. Expression of caldesmon interferes with Rho
A-V14-mediated formation of focal adhesions and stress fibers as well
as with formation of focal adhesions induced by microtubule disruption. This inhibitory effect depends on the actin- and myosin-binding regions
of caldesmon, because a truncated variant lacking both of these regions
is inactive. The effects of caldesmon are blocked by the ionophore
A23187, thapsigargin, and membrane depolarization, presumably because
of the ability of Ca2+-calmodulin or
Ca2+-S100 proteins to antagonize the inhibitory function
of caldesmon on actomyosin contraction. These results indicate a role
for nonmuscle caldesmon in the physiological regulation of actomyosin
contractility and adhesion-dependent signaling and further demonstrate
the involvement of contractility in focal adhesion formation.
Molecular Cell Biology and
§Materials and Interfaces, The Weizmann Institute of
Science, Rehovot 76100, Israel
These authors contributed equally to this work.
Corresponding author. E-mail address:
libersha{at}weizmann.weizmann.ac.il.
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