This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lai, Y.-J.
Right arrow Articles by Lin, F.-T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lai, Y.-J.
Right arrow Articles by Lin, F.-T.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, July 2005, p. 5859-5868, Vol. 25, No. 14
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.14.5859-5868.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

c-Src-Mediated Phosphorylation of TRIP6 Regulates Its Function in Lysophosphatidic Acid-Induced Cell Migration{dagger}

Yun-Ju Lai,1 Chen-Shan Chen,1 Weei-Chin Lin,1,2 and Fang-Tsyr Lin1*

Department of Cell Biology,1 Division of Hematology and Oncology, Department of Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294-00052

Received 13 September 2004/ Returned for modification 26 November 2004/ Accepted 11 April 2005

TRIP6 (thyroid receptor-interacting protein 6), also known as ZRP-1 (zyxin-related protein 1), is a member of the zyxin family that has been implicated in cell motility. Previously we have shown that TRIP6 binds to the LPA2 receptor and associates with several components of focal complexes in an agonist-dependent manner and, thus, enhances lysophosphatidic acid (LPA)-induced cell migration. Here we further report that the function of TRIP6 in LPA signaling is regulated by c-Src-mediated phosphorylation of TRIP6 at the Tyr-55 residue. LPA stimulation induces tyrosine phosphorylation of endogenous TRIP6 in NIH 3T3 cells and c-Src-expressing fibroblasts, which is virtually eliminated in Src-null fibroblasts. Strikingly, both phosphotyrosine-55 and proline-58 residues of TRIP6 are required for Crk binding in vitro and in cells. Mutation of Tyr-55 to Phe does not alter the ability of TRIP6 to localize at focal adhesions or associate with actin. However, it abolishes the association of TRIP6 with Crk and p130cas in cells and significantly reduces the function of TRIP6 to promote LPA-induced ERK activation. Ultimately, these signaling events control TRIP6 function in promoting LPA-induced morphological changes and cell migration.

* Corresponding author. Mailing address: MCLM 360A, 1918 University Blvd., Birmingham, AL 35294-0005. Phone: (205) 975-5060. Fax: (205) 975-5648. E-mail: flin{at}uab.edu.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

Molecular and Cellular Biology, July 2005, p. 5859-5868, Vol. 25, No. 14
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.14.5859-5868.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • E, S., Lai, Y.-J., Tsukahara, R., Chen, C.-S., Fujiwara, Y., Yue, J., Yu, J.-H., Guo, H., Kihara, A., Tigyi, G., Lin, F.-T. (2009). Lysophosphatidic Acid 2 Receptor-mediated Supramolecular Complex Formation Regulates Its Antiapoptotic Effect. J. Biol. Chem. 284: 14558-14571 [Abstract] [Full Text]  
  • Chastre, E., Abdessamad, M., Kruglov, A., Bruyneel, E., Bracke, M., Di Gioia, Y., Beckerle, M. C., van Roy, F., Kotelevets, L. (2009). TRIP6, a novel molecular partner of the MAGI-1 scaffolding molecule, promotes invasiveness. FASEB J. 23: 916-928 [Abstract] [Full Text]  
  • Crowley, J. L., Smith, T. C., Fang, Z., Takizawa, N., Luna, E. J. (2009). Supervillin Reorganizes the Actin Cytoskeleton and Increases Invadopodial Efficiency. Mol. Biol. Cell 20: 948-962 [Abstract] [Full Text]  
  • Lai, Y.-J., Lin, W.-C., Lin, F.-T. (2007). PTPL1/FAP-1 Negatively Regulates TRIP6 Function in Lysophosphatidic Acid-induced Cell Migration. J. Biol. Chem. 282: 24381-24387 [Abstract] [Full Text]  
  • Bai, C.-Y., Ohsugi, M., Abe, Y., Yamamoto, T. (2007). ZRP-1 controls Rho GTPase-mediated actin reorganization by localizing at cell-matrix and cell-cell adhesions. J. Cell Sci. 120: 2828-2837 [Abstract] [Full Text]  
  • Worley, M. J., Nieman, G. S., Geddes, K., Heffron, F. (2006). Salmonella typhimurium disseminates within its host by manipulating the motility of infected cells. Proc. Natl. Acad. Sci. USA 103: 17915-17920 [Abstract] [Full Text]  
  • Wang, Q., Lu, R., Zhao, J., Limbird, L. E. (2006). Arrestin Serves as a Molecular Switch, Linking Endogenous {alpha}2-Adrenergic Receptor to SRC-dependent, but Not SRC-independent, ERK Activation. J. Biol. Chem. 281: 25948-25955 [Abstract] [Full Text]  
  • Takizawa, N., Smith, T. C., Nebl, T., Crowley, J. L., Palmieri, S. J., Lifshitz, L. M., Ehrhardt, A. G., Hoffman, L. M., Beckerle, M. C., Luna, E. J. (2006). Supervillin modulation of focal adhesions involving TRIP6/ZRP-1. JCB 174: 447-458 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»