|
|
|
|
|
|
|
|
|||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
First published online 12 February 2003
doi: 10.1242/jcs.00309
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Research Article |
-actinin
1 ITI Research Institute, University of Bern, PO Box 54, CH-3010 Bern,
Switzerland
2 Institute for Clinical Biochemistry and Pathobiochemistry, University of
Würzburg, Versbacher Strasse 5, D-97078 Würzburg, Germany
* Author for correspondence (e-mail: beat.trueb{at}iti.unibe.ch)
Accepted 4 December 2002
The lipoma preferred partner LPP is a member of the zyxin family of
proteins. In this paper, we demonstrate that the structural similarities
observed between zyxin and LPP also extend to their interaction capabilities.
Similar to zyxin, LPP was found to bind to 
-actinin in vitro. This
interaction was confirmed in yeast and mammalian cells. Studies utilizing the
three-hybrid system further indicated that zyxin and LPP compete for the same
binding site in -actinin. This site was mapped to the central rod of
-actinin, which contains spectrin-like repeats 2 and 3. In the case of
LPP, a conserved motif present at the N-terminus was shown to be responsible
for the interaction. Constructs lacking this motif did not bind to
-actinin in the yeast two-hybrid system and were not able to recruit
-actinin to an ectopic site in mammalian cells. Quantitative data
obtained with the two-hybrid and the three-hybrid system suggest that LPP has
a lower affinity for -actinin than zyxin. It is likely that this
difference leads to slightly different roles played by LPP and zyxin during
the assembly and disassembly of focal adhesions.
Key words: -Actinin, Cytoskeleton, Focal adhesion, Lipoma preferred partner, LPP, Zyxin
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati 
Twitter What's this?
This article has been cited by other articles:
|
|
 |
|
  M. M.R. Petit, H. Lindskog, E. Larsson, P. Wasteson, E. Athley, S. Breuer, M. Angstenberger, D. Hertfelder, E. Mattsson, A. Nordheim, et al. Smooth Muscle Expression of Lipoma Preferred Partner Is Mediated by an Alternative Intronic Promoter That Is Regulated by Serum Response Factor/Myocardin Circ. Res., July 3, 2008; 103(1): 61 - 69. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C.-Y. Bai, M. Ohsugi, Y. Abe, and T. Yamamoto ZRP-1 controls Rho GTPase-mediated actin reorganization by localizing at cell-matrix and cell-cell adhesions J. Cell Sci., August 15, 2007; 120(16): 2828 - 2837. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Guo, R. E. Sallis, A. Greenall, M. M. R. Petit, E. Jansen, L. Young, W. J. M. Van de Ven, and A. D. Sharrocks The LIM Domain Protein LPP Is a Coactivator for the ETS Domain Transcription Factor PEA3 Mol. Cell. Biol., June 15, 2006; 26(12): 4529 - 4538. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y.-J. Lai, C.-S. Chen, W.-C. Lin, and F.-T. Lin c-Src-Mediated Phosphorylation of TRIP6 Regulates Its Function in Lysophosphatidic Acid-Induced Cell Migration Mol. Cell. Biol., July 15, 2005; 25(14): 5859 - 5868. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Li, L. Zhuang, and B. Trueb Zyxin Interacts with the SH3 Domains of the Cytoskeletal Proteins LIM-nebulette and Lasp-1 J. Biol. Chem., May 7, 2004; 279(19): 20401 - 20410. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 I. Gorenne, R. K. Nakamoto, C. P. Phelps, M. C. Beckerle, A. V. Somlyo, and A. P. Somlyo LPP, a LIM protein highly expressed in smooth muscle Am J Physiol Cell Physiol, September 1, 2003; 285(3): C674 - C685. [Abstract] [Full Text] [PDF]
|
|
