Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M300425200 on February 5, 2003

J. Biol. Chem., Vol. 278, Issue 16, 14274-14283, April 18, 2003
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
278/16/14274    most recent
M300425200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Duchesne, C.
Right arrow Articles by Rivard, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Duchesne, C.
Right arrow Articles by Rivard, N.
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  
What's this?

Negative Regulation of beta -Catenin Signaling by Tyrosine Phosphatase SHP-1 in Intestinal Epithelial Cells*

Cathia DuchesneDagger §, Stéphanie CharlandDagger §, Claude Asselin, Clara Nahmias||, and Nathalie RivardDagger **

From the Dagger  Département d'Anatomie et Biologie Cellulaire, Faculté de Médecine, Université de Sherbrooke, Sherbrooke, Québec J1H 5N4, Canada and the || Department of Cell Biology, Institut Cochin, 75014 Paris, France

Protein-tyrosine phosphatase SHP-1 is expressed at high levels in hematopoietic cells and at moderate levels in many other cell types including epithelial cells. Although SHP-1 has been shown to be a negative regulator of multiple signaling pathways in hematopoietic cells, very little is known about the biological role of SHP-1 in epithelial cells. In order to elucidate the mechanism(s) responsible for the loss of proliferative potential once committed intestinal epithelial cells begin to differentiate, the role and regulation of SHP-1 were analyzed in both intact epithelium as well as in well established intestinal cell models recapitulating the crypt-villus axis in vitro. Results show that SHP-1 was expressed in the nuclei of all intestinal epithelial cell models as well as in epithelial cells of intact human fetal jejunum and colon. Expression and phosphatase activity levels of SHP-1 were much more elevated in confluent growth-arrested intestinal epithelial cells and in differentiated enterocytes as well. Overexpression of SHP-1 in intestinal epithelial crypt cells significantly inhibited dhfr, c-myc, and cyclin D1 gene expression but did not interfere with c-fos gene expression. In contrast, a mutated inactive form of SHP-1 had no effect on these genes. SHP-1 expression significantly decreased beta -catenin/TCF-dependent transcription in intestinal epithelial crypt cells. Immunoprecipitation experiments revealed that beta -catenin is one of the main binding partners and a substrate for SHP-1. Taken together, our results indicate that SHP-1 may be involved in the regulation of beta -catenin transcriptional function and in the negative control of intestinal epithelial cell proliferation.

* This work was supported in part by a grant from the Natural Sciences and Engineering Research Council of Canada.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Both authors contributed equally to this work.

Student scholar from the Fonds pour la Recherche en Santé du Québec.

** Recipient of a Canadian Research Chair in Signaling and Digestive Physiopathology. To whom correspondence should be addressed: Dépt. of d'Anatomie et de Biologie Cellulaire, Faculté de Médecine, Université de Sherbrooke, Sherbrooke, Quebec J1H 5N4, Canada. Tel.: 819-564-5271; Fax: 819-564-5320; E-mail: Nathalie.Rivard@USherbrooke.ca.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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    What's this?


This article has been cited by other articles:


Home page
 FASEB J.Home page
M.-J. Langlois, S. A. B. Roy, B. A. Auclair, C. Jones, F. Boudreau, J. C. Carrier, N. Rivard, and N. Perreault
Epithelial phosphatase and tensin homolog regulates intestinal architecture and secretory cell commitment and acts as a modifier gene in neoplasia
FASEB J, June 1, 2009; 23(6): 1835 - 1844.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Simoneau, J. Boulanger, G. Coulombe, M.-A. Renaud, C. Duchesne, and N. Rivard
Activation of Cdk2 Stimulates Proteasome-dependent Truncation of Tyrosine Phosphatase SHP-1 in Human Proliferating Intestinal Epithelial Cells
J. Biol. Chem., September 12, 2008; 283(37): 25544 - 25556.
[Abstract] [Full Text] [PDF]

Home page
 FASEB J.Home page
T. Voisin, A. El Firar, C. Rouyer-Fessard, V. Gratio, and M. Laburthe
A hallmark of immunoreceptor, the tyrosine-based inhibitory motif ITIM, is present in the G protein-coupled receptor OX1R for orexins and drives apoptosis: a novel mechanism
FASEB J, June 1, 2008; 22(6): 1993 - 2002.
[Abstract] [Full Text] [PDF]

Home page
 J. Leukoc. Biol.Home page
Y. Liu, M. J. Kruhlak, J.-J. Hao, and S. Shaw
Rapid T cell receptor-mediated SHP-1 S591 phosphorylation regulates SHP-1 cellular localization and phosphatase activity
J. Leukoc. Biol., September 1, 2007; 82(3): 742 - 751.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
L. Anders, P. Mertins, S. Lammich, M. Murgia, D. Hartmann, P. Saftig, C. Haass, and A. Ullrich
Furin-, ADAM 10-, and {gamma}-Secretase-Mediated Cleavage of a Receptor Tyrosine Phosphatase and Regulation of {beta}-Catenin's Transcriptional Activity
Mol. Cell. Biol., May 15, 2006; 26(10): 3917 - 3934.
[Abstract] [Full Text] [PDF]

Home page
 GutHome page
J Schnekenburger, J Mayerle, B Kruger, I Buchwalow, F U Weiss, E Albrecht, V E Samoilova, W Domschke, and M M Lerch
Protein tyrosine phosphatase {kappa} and SHP-1 are involved in the regulation of cell-cell contacts at adherens junctions in the exocrine pancreas
Gut, October 1, 2005; 54(10): 1445 - 1455.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. Roccato, C. Miranda, G. Raho, S. Pagliardini, M. A. Pierotti, and A. Greco
Analysis of SHP-1-mediated Down-regulation of the TRK-T3 Oncoprotein Identifies Trk-fused Gene (TFG) as a Novel SHP-1-interacting Protein
J. Biol. Chem., February 4, 2005; 280(5): 3382 - 3389.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
A. E. Moran, A. M. Carothers, M. J. Weyant, M. Redston, and M. M. Bertagnolli
Carnosol Inhibits {beta}-Catenin Tyrosine Phosphorylation and Prevents Adenoma Formation in the C57BL/6J/Min/+ (Min/+) Mouse
Cancer Res., February 1, 2005; 65(3): 1097 - 1104.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement