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First published online 21 September 2004
doi: 10.1242/jcs.01378

Journal of Cell Science 117, 5043-5057 (2004)
Published by The Company of Biologists 2004
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Research Article

Smooth muscle archvillin: a novel regulator of signaling and contractility in vascular smooth muscle

Samudra S. Gangopadhyay1, Norio Takizawa2, Cynthia Gallant1, Amy L. Barber1, Hyun-Dong Je1, Tara C. Smith2, Elizabeth J. Luna2 and Kathleen G. Morgan1,3,*

1 Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA
2 Cell Dynamics Group, Department of Cell Biology, University of Massachusetts Medical School, 55 Lake Avenue, Worcester, MA 01605, USA
3 Department of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Avenue, Boston, MA 02215, USA

* Author for correspondence (e-mail: morgan{at}bbri.org)

Accepted 24 June 2004

The mechanisms by which protein kinase C (PKC) and extracellular-signal-regulated kinases (ERK1/2) govern smooth-muscle contractility remain unclear. Calponin (CaP), an actin-binding protein and PKC substrate, mediates signaling through ERK1/2. We report here that CaP sequences containing the CaP homology (CH) domain bind to the C-terminal 251 amino acids of smooth-muscle archvillin (SmAV), a new splice variant of supervillin, which is a known actin- and myosin-II-binding protein. The CaP-SmAV interaction is demonstrated by reciprocal yeast two-hybrid and blot-overlay assays and by colocalization in COS-7 cells. In differentiated smooth muscle, endogenous SmAV and CaP co-fractionate and co-translocate to the cell cortex after stimulation by agonist. Antisense knockdown of SmAV in tissue inhibits both the activation of ERK1/2 and contractions stimulated by either agonist or PKC activation. This ERK1/2 signaling and contractile defect is similar to that observed in CaP knockdown experiments. In A7r5 smooth-muscle cells, PKC activation by phorbol esters induces the reorganization of endogenous, membrane-localized SmAV and microfilament-associated CaP into podosome-like structures that also contain F-actin, nonmuscle myosin IIB and ERK1/2. These results indicate that SmAV contributes to the regulation of contractility through a CaP-mediated signaling pathway, involving PKC activation and phosphorylation of ERK1/2.

Key words: Supervillin, Calponin, PKC, ERK, Podosome


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