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Vol. 14, Issue 6, 2482-2491, June 2003
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Institute of Molecular Biology, Department of Cell Biology, Austrian Academy of Sciences, A-5020 Salzburg, Austria
Submitted November 18, 2002;
Revised December 11, 2002;
Accepted January 30, 2003
Monitoring Editor: David Drubin
Phorbol ester induces actin cytoskeleton rearrangements in cultured
vascular smooth muscle cells. Calponin and SM22 
are major components
of differentiated smooth muscle and potential regulators of actin cytoskeleton
interactions. Here we show that actin fibers decorated with h1 CaP
remain stable, whereas SM22 -decorated actin bundles undergo rapid
reorganization into podosomes within 30 min of PDBu exposure. Ectopic
expression of GFP -actinin had no effect on the stability of the actin
cytoskeleton and -actinin was transported rapidly into PDBu-induced
podosomes. Our results demonstrate the involvement of CaP and SM22 in
coordinating the balance between stabilization and dynamics of the actin
cytoskeleton in mammalian smooth muscle. We provide evidence for the existence
of two functionally distinct actin filament populations and introduce a
molecular mechanism for the stabilization of the actin cytoskeleton by the
unique actin-binding interface formed by calponin family-specific
CLIK23 repeats.
Online version of this article contains video material. Online version is
available at
www.molbiolcell.org.
* Corresponding author. E-mail address: mgimona{at}server1.imolbio.oeaw.ac.at.
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