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A more recent version of this article appeared on June 1, 2003
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Submitted on November 18, 2002
Revised on December 11, 2002
Accepted on December 31, 2002
1 Institute of Molecular Biology, Department of Cell Biology, Austrian Academy of Sciences, Billrothstrasse 11, A-5020 Salzburg, AUSTRIA
* Corresponding author. E-mail address: mgimona{at}server1.imolbio.oeaw.ac.at.
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 while SM22 -decorated actin bundles undergo rapid reorganization into podosomes within 30 minutes 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.
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