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


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search    

The fully linked HTML version of this article has now been published.
JCS ePress online publication date 29 Jun 2004
doi: 10.1242/jcs.01216

This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
jcs.01216v1
jcs.01216v2
117/16/3593    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 Li, Y.
Right arrow Articles by Lin, J. J.C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Li, Y.
Right arrow Articles by Lin, J. J.C.
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

Caldesmon mutant defective in Ca2+-calmodulin binding interferes with assembly of stress fibers and affects cell morphology, growth and motility


Yan Li, Jenny L.C. Lin, Rebecca S. Reiter, Karla Daniels, David R. Soll, and Jim J.C. Lin*
* Author for correspondence (e-mail: jim-lin{at}uiowa.edu)

Despite intensive in vitro studies, little is known about the regulation of caldesmon (CaD) by Ca2+-calmodulin (Ca2+-CaM) in vivo. To investigate this regulation, a mutant was generated of the C-terminal fragment of human fibroblast CaD, termed CaD39-AB, in which two crucial tryptophan residues involved in Ca2+-CaM binding were each replaced with alanine. The mutation abolished most CaD39-AB binding to Ca2+-CaM in vitro but had little effect on in vitro binding to actin filaments and the ability to inhibit actin/tropomyosin-activated heavy meromyosin ATPase. To study the functional consequences of these mutations in vivo, we transfected an expression plasmid carrying CaD39-AB cDNA into Chinese hamster ovary (CHO) cells and isolated several clones expressing various amounts of CaD39-AB. Immunofluorescence microscopy revealed that mutant CaD39-AB was distributed diffusely throughout the cytoplasm but also concentrated at membrane ruffle regions. Stable expression of CaD39-AB in CHO cells disrupted assembly of stress fibers and focal adhesions, altered cell morphology, and slowed cell cycle progression. Moreover, CaD39-AB-expressing cells exhibited motility defects in a wound-healing assay, in both velocity and the persistence of translocation, suggesting a role for CaD regulation by Ca2+-CaM in cell migration. Together, these results demonstrate that CaD plays a crucial role in mediating the effects of Ca2+-CaM on the dynamics of the actin cytoskeleton during cell migration.
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 R Soc InterfaceHome page
F. Kantawong, R. Burchmore, N. Gadegaard, R. O. C. Oreffo, and M. J. Dalby
Proteomic analysis of human osteoprogenitor response to disordered nanotopography
J R Soc Interface, November 6, 2009; 6(40): 1075 - 1086.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Mayanagi, T. Morita, K. Hayashi, K. Fukumoto, and K. Sobue
Glucocorticoid Receptor-mediated Expression of Caldesmon Regulates Cell Migration via the Reorganization of the Actin Cytoskeleton
J. Biol. Chem., November 7, 2008; 283(45): 31183 - 31196.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
K. Thorsen, K. D. Sorensen, A. S. Brems-Eskildsen, C. Modin, M. Gaustadnes, A.-M. K. Hein, M. Kruhoffer, S. Laurberg, M. Borre, K. Wang, et al.
Alternative Splicing in Colon, Bladder, and Prostate Cancer Identified by Exon Array Analysis
Mol. Cell. Proteomics, July 1, 2008; 7(7): 1214 - 1224.
[Abstract] [Full Text] [PDF]

Home page
 Mol Hum ReprodHome page
P. A. Fowler, N. J. Dora, H. McFerran, M. R. Amezaga, D. W. Miller, R. G. Lea, P. Cash, A. S. McNeilly, N. P. Evans, C. Cotinot, et al.
In utero exposure to low doses of environmental pollutants disrupts fetal ovarian development in sheep
Mol. Hum. Reprod., May 1, 2008; 14(5): 269 - 280.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Respir. Cell Mol. Bio.Home page
S. E. McGowan, A. J. Holmes, R. P. Mecham, and T. M. Ritty
Arg-Gly-Asp-Containing Domains of Fibrillins-1 and -2 Distinctly Regulate Lung Fibroblast Migration
Am. J. Respir. Cell Mol. Biol., April 1, 2008; 38(4): 435 - 445.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Choi, E. A. Gustafson-Wagner, Q. Wang, S. M. Harlan, H. W. Sinn, J. L.-C. Lin, and J. J.-C. Lin
The Intercalated Disc Protein, mXin{alpha}, Is Capable of Interacting with -Catenin and Bundling Actin Filaments
J. Biol. Chem., December 7, 2007; 282(49): 36024 - 36036.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
T. Morita, T. Mayanagi, and K. Sobue
Dual roles of myocardin-related transcription factors in epithelial mesenchymal transition via slug induction and actin remodeling
J. Cell Biol., December 3, 2007; 179(5): 1027 - 1042.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
R. Eves, B. A. Webb, S. Zhou, and A. S. Mak
Caldesmon is an integral component of podosomes in smooth muscle cells
J. Cell Sci., May 1, 2006; 119(9): 1691 - 1702.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. E. Cuomo, A. Knebel, G. Platt, N. Morrice, P. Cohen, and S. Mittnacht
Regulation of Microfilament Organization by Kaposi Sarcoma-associated Herpes Virus-cyclin{middle dot}CDK6 Phosphorylation of Caldesmon
J. Biol. Chem., October 28, 2005; 280(43): 35844 - 35858.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2004