spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

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
This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
jcs.01378v1
117/21/5043    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gangopadhyay, S. S.
Right arrow Articles by Morgan, K. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gangopadhyay, S. S.
Right arrow Articles by Morgan, K. G.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

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


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
S. S. Gangopadhyay, E. Kengni, S. Appel, C. Gallant, H. R. Kim, P. Leavis, J. DeGnore, and K. G. Morgan
Smooth Muscle Archvillin Is an ERK Scaffolding Protein
J. Biol. Chem., June 26, 2009; 284(26): 17607 - 17615.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
J. L. Crowley, T. C. Smith, Z. Fang, N. Takizawa, and E. J. Luna
Supervillin Reorganizes the Actin Cytoskeleton and Increases Invadopodial Efficiency
Mol. Biol. Cell, February 1, 2009; 20(3): 948 - 962.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
N. Takizawa, R. Ikebe, M. Ikebe, and E. J. Luna
Supervillin slows cell spreading by facilitating myosin II activation at the cell periphery
J. Cell Sci., November 1, 2007; 120(21): 3792 - 3803.
[Abstract] [Full Text] [PDF]

Home page
 Genome ResHome page
S. J. Cooper, N. D. Trinklein, L. Nguyen, and R. M. Myers
Serum response factor binding sites differ in three human cell types
Genome Res., February 1, 2007; 17(2): 136 - 144.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
N. Takizawa, T. C. Smith, T. Nebl, J. L. Crowley, S. J. Palmieri, L. M. Lifshitz, A. G. Ehrhardt, L. M. Hoffman, M. C. Beckerle, and E. J. Luna
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
J. Cell Biol., July 31, 2006; 174(3): 447 - 458.
[Abstract] [Full Text] [PDF]

Home page
 Circ. Res.Home page
W. A. Marganski, S. S. Gangopadhyay, H.-D. Je, C. Gallant, and K. G. Morgan
Targeting of a Novel Ca+2/Calmodulin-Dependent Protein Kinase II Is Essential for Extracellular Signal-Regulated Kinase-Mediated Signaling in Differentiated Smooth Muscle Cells
Circ. Res., September 16, 2005; 97(6): 541 - 549.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
C. Gallant, J. Y. You, Y. Sasaki, Z. Grabarek, and K. G. Morgan
MARCKS is a major PKC-dependent regulator of calmodulin targeting in smooth muscle
J. Cell Sci., August 15, 2005; 118(16): 3595 - 3605.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2004