Molecular Biology of the Cell click for CBE Life Science Education Page

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

Originally published as MBC in Press, 10.1091/mbc.E06-03-0179 on December 27, 2006

Vol. 18, Issue 3, 910-918, March 2007

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E06-03-0179v1
18/3/910    most recent
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kroboth, K.
Right arrow Articles by Näthke, I. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kroboth, K.
Right arrow Articles by Näthke, I. S.

Lack of Adenomatous Polyposis Coli Protein Correlates with a Decrease in Cell Migration and Overall Changes in Microtubule StabilityFormula

Karin Kroboth*, Ian P. Newton*, Katsuhiro Kita{dagger}, Dina Dikovskaya*, Jürg Zumbrunn*,{ddagger}, Clare M. Waterman-Storer{dagger}, and Inke S. Näthke*

*Division of Cell and Developmental Biology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom; and {dagger}Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037

Submitted March 6, 2006; Revised December 4, 2006; Accepted December 18, 2006
Monitoring Editor: Paul Forscher

Most sporadic colorectal tumors carry truncation mutations in the adenomatous polyposis coli (APC) gene. The APC protein is involved in many processes that govern gut tissue. In addition to its involvement in the regulation of beta-catenin, APC is a cytoskeletal regulator with direct and indirect effects on microtubules. Cancer-related truncation mutations lack direct and indirect binding sites for microtubules in APC, suggesting that loss of this function contributes to defects in APC-mutant cells. In this study, we show that loss of APC results in disappearance of cellular protrusions and decreased cell migration. These changes are accompanied by a decrease in overall microtubule stability and also by a decrease in posttranslationally modified microtubules in the cell periphery particularly the migrating edge. Consistent with the ability of APC to affect cell shape, the overexpression of APC in cells can induce cellular protrusions. These data demonstrate that cell migration and microtubule stability are linked to APC status, thereby revealing a weakness in APC-deficient cells with potential therapeutic implications.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-03-0179) on December 27, 2006.

Formula The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

{ddagger} Present address: Polyphor Ltd., Gewerbestrasse 14, CH-4123 Allschwil, Switzerland.

Address correspondence to: Inke S. Näthke (inke{at}lifesci.dundee.ac.uk)




This article has been cited by other articles:


Home page
 J. Cell Sci.Home page
P. Murawala, M. M. Tripathi, P. Vyas, A. Salunke, and J. Joseph
Nup358 interacts with APC and plays a role in cell polarization
J. Cell Sci., September 1, 2009; 122(17): 3113 - 3122.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
T. Zhang, K. J. M. Zaal, J. Sheridan, A. Mehta, G. G. Gundersen, and E. Ralston
Microtubule plus-end binding protein EB1 is necessary for muscle cell differentiation, elongation and fusion
J. Cell Sci., May 1, 2009; 122(9): 1401 - 1409.
[Abstract] [Full Text] [PDF]

Home page
 DevelopmentHome page
R. L. Webb, M.-N. Zhou, and B. M. McCartney
A novel role for an APC2-Diaphanous complex in regulating actin organization in Drosophila
Development, April 15, 2009; 136(8): 1283 - 1293.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Matsui, S. Kaieda, T. Ikegami, and Y. Mimori-Kiyosue
Identification of a Link between the SAMP Repeats of Adenomatous Polyposis Coli Tumor Suppressor and the Src Homology 3 Domain of DDEF
J. Biol. Chem., November 21, 2008; 283(47): 33006 - 33020.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
Z. Li, K. Kroboth, I. P. Newton, and I. S. Nathke
Novel self-association of the APC molecule affects APC clusters and cell migration
J. Cell Sci., June 1, 2008; 121(11): 1916 - 1925.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
M. P. Koester, O. Muller, and G. E. Pollerberg
Adenomatous Polyposis Coli Is Differentially Distributed in Growth Cones and Modulates Their Steering
J. Neurosci., November 14, 2007; 27(46): 12590 - 12600.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
A. Grohmann, K. Tanneberger, A. Alzner, J. Schneikert, and J. Behrens
AMER1 regulates the distribution of the tumor suppressor APC between microtubules and the plasma membrane
J. Cell Sci., November 1, 2007; 120(21): 3738 - 3747.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
K. Aoki and M. M. Taketo
Adenomatous polyposis coli (APC): a multi-functional tumor suppressor gene
J. Cell Sci., October 1, 2007; 120(19): 3327 - 3335.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2007 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.