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Vol. 11, Issue 10, 3617-3627, October 2000
Laboratory of Molecular Cardiology, National Heart, Lung, and Blood
Institute, National Institutes of Health, Bethesda, Maryland 20892
A truncated fragment of the nonmuscle myosin II-A heavy chain (NMHC
II-A) lacking amino acids 1-591, 
N592, was used to examine the
cellular functions of this protein. Green fluorescent protein (GFP) was
fused to the amino terminus of full-length human NMHC II-A, NMHC II-B,
and N592 and the fusion proteins were stably expressed in HeLa cells
by using a conditional expression system requiring absence of
doxycycline. The HeLa cell line studied normally expressed only NMHC
II-A and not NMHC II-B protein. Confocal microscopy indicated that the
GFP fusion proteins of full-length NMHC II-A, II-B, and N592 were
localized to stress fibers. However, in vitro assays showed that
baculovirus-expressed N592 did not bind to actin, suggesting that
N592 was localized to actin stress fibers through incorporation into
endogenous myosin filaments. There was no evidence for the formation of
heterodimers between the full-length endogenous nonmuscle myosin and
truncated nonmuscle MHCs. Expression of N592, but not full-length
NMHC II-A or NMHC II-B, induced cell rounding with rearrangement of
actin filaments and disappearance of focal adhesions. These cells
returned to their normal morphology when expression of N592 was
repressed by addition of doxycycline. We also show that GFP-tagged
full-length NMHC II-A or II-B, but not N592, were localized to the
cytokinetic ring during mitosis, indicating that, in vertebrates, the
amino-terminus part of mammalian nonmuscle myosin II may be necessary
for localization to the cytokinetic ring.
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