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TRIP6, a novel molecular partner of the MAGI-1 scaffolding molecule, promotes invasiveness

Eric Chastre, Mahmoud Abdessamad, Alexey Kruglov, Erik Bruyneel, Marc Bracke UGent, Yolande Di Gioia, Mary C. Beckerle, Frans Van Roy UGent and Larissa Kotelevets (2009) FASEB JOURNAL. 23(3). p.916-928
abstract
We recently established the critical role of the PTEN/MAGI-1b signalosome in stabilization of cell-cell contacts and suppression of invasiveness. The PTEN tumor suppressor is recruited to E-cadherin junctional complexes through the binding to the second PDZ domain of the MAGI-1b scaffolding molecule, whereas beta-catenin interacts with the fifth PDZ domain. To identify additional effectors of this signalosome, we used yeast 2-hybrid screening. Among the clones identified, we focused on TRIP6, which belongs to the zyxin family of proteins. We demonstrated that TRIP6 interacted directly with MAGI-1b by binding to its fifth PDZ domain. Ectopic expression of TRIP6 induced invasiveness in the epithelial MDCK and MDCKts-src cells in a PI3-kinase-and a NF-kappa B-dependent manner and impaired cell-cell aggregation at least in part by uncoupling adherens junctional complexes from the cytoskeleton. The TRIP6Stop473 mutant, which lacks the PDZ binding motif, was still able to increase NF-kappa B and Akt activities but did not promote invasiveness or interfere with cell-cell aggregation. Intracellular delivery of competing peptides corresponding to TRIP6 or beta-catenin C terminus restored invasive properties in MDCKts-src TRIP6Stop473 cells, highlighting the requirement of PDZ scaffolds in junctional complexes activity. TRIP6 overexpression in colon tumors suggest its critical role in cancer progression.-Chastre, E., Abdessamad, M., Kruglov, A., Bruyneel, E., Bracke, M., Di Gioia, Y., Beckerle, M. C., van Roy, F., Kotelevets, L. TRIP6, a novel molecular partner of the MAGI-1 scaffolding molecule, promotes invasiveness.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
journal title
FASEB JOURNAL
volume
23
issue
3
pages
916 - 928
Web of Science type
Article
Web of Science id
000265506300027
JCR category
BIOLOGY
JCR impact factor
6.401 (2009)
JCR rank
3/73 (2009)
JCR quartile
1 (2009)
ISSN
0892-6638
DOI
10.1096/fj.08-106344
language
English
UGent publication?
yes
classification
A1
id
632599
handle
http://hdl.handle.net/1854/LU-632599
date created
2009-05-19 12:24:56
date last changed
2012-06-26 14:31:43
@article{632599,
  abstract     = {We recently established the critical role of the PTEN/MAGI-1b signalosome in stabilization of cell-cell contacts and suppression of invasiveness. The PTEN tumor suppressor is recruited to E-cadherin junctional complexes through the binding to the second PDZ domain of the MAGI-1b scaffolding molecule, whereas beta-catenin interacts with the fifth PDZ domain. To identify additional effectors of this signalosome, we used yeast 2-hybrid screening. Among the clones identified, we focused on TRIP6, which belongs to the zyxin family of proteins. We demonstrated that TRIP6 interacted directly with MAGI-1b by binding to its fifth PDZ domain. Ectopic expression of TRIP6 induced invasiveness in the epithelial MDCK and MDCKts-src cells in a PI3-kinase-and a NF-kappa B-dependent manner and impaired cell-cell aggregation at least in part by uncoupling adherens junctional complexes from the cytoskeleton. The TRIP6Stop473 mutant, which lacks the PDZ binding motif, was still able to increase NF-kappa B and Akt activities but did not promote invasiveness or interfere with cell-cell aggregation. Intracellular delivery of competing peptides corresponding to TRIP6 or beta-catenin C terminus restored invasive properties in MDCKts-src TRIP6Stop473 cells, highlighting the requirement of PDZ scaffolds in junctional complexes activity. TRIP6 overexpression in colon tumors suggest its critical role in cancer progression.-Chastre, E., Abdessamad, M., Kruglov, A., Bruyneel, E., Bracke, M., Di Gioia, Y., Beckerle, M. C., van Roy, F., Kotelevets, L. TRIP6, a novel molecular partner of the MAGI-1 scaffolding molecule, promotes invasiveness.},
  author       = {Chastre, Eric and Abdessamad, Mahmoud and Kruglov, Alexey and Bruyneel, Erik and Bracke, Marc and Di Gioia, Yolande and Beckerle, Mary C. and Van Roy, Frans and Kotelevets, Larissa},
  issn         = {0892-6638},
  journal      = {FASEB JOURNAL},
  language     = {eng},
  number       = {3},
  pages        = {916--928},
  title        = {TRIP6, a novel molecular partner of the MAGI-1 scaffolding molecule, promotes invasiveness},
  url          = {http://dx.doi.org/10.1096/fj.08-106344},
  volume       = {23},
  year         = {2009},
}

Chicago
Chastre, Eric, Mahmoud Abdessamad, Alexey Kruglov, Erik Bruyneel, Marc Bracke, Yolande Di Gioia, Mary C. Beckerle, Frans Van Roy, and Larissa Kotelevets. 2009. “TRIP6, a Novel Molecular Partner of the MAGI-1 Scaffolding Molecule, Promotes Invasiveness.” Faseb Journal 23 (3): 916–928.
APA
Chastre, E., Abdessamad, M., Kruglov, A., Bruyneel, E., Bracke, M., Di Gioia, Y., Beckerle, M. C., et al. (2009). TRIP6, a novel molecular partner of the MAGI-1 scaffolding molecule, promotes invasiveness. FASEB JOURNAL, 23(3), 916–928.
Vancouver
1.
Chastre E, Abdessamad M, Kruglov A, Bruyneel E, Bracke M, Di Gioia Y, et al. TRIP6, a novel molecular partner of the MAGI-1 scaffolding molecule, promotes invasiveness. FASEB JOURNAL. 2009;23(3):916–28.
MLA
Chastre, Eric, Mahmoud Abdessamad, Alexey Kruglov, et al. “TRIP6, a Novel Molecular Partner of the MAGI-1 Scaffolding Molecule, Promotes Invasiveness.” FASEB JOURNAL 23.3 (2009): 916–928. Print.