Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Subscribe

Sci. Signal., 4 September 2012
Vol. 5, Issue 240, p. ra64
[DOI: 10.1126/scisignal.2002871]

RESEARCH ARTICLES

Editor's Summary

The Microtubule Regulator in the Family
Mutations in the tumor suppressor WTX, which is also known as FAM123B, are associated with Wilms disease in children. To better define the cellular functions of the other members of the FAM123 family, Siesser et al. characterized the protein-protein interaction networks for FAM123A, WTX, and FAM123C and found that in contrast to the other FAM123 family members, FAM123A interacted with microtubule-associated proteins. Biochemical, cellular, and imaging assays indicated that FAM123A altered microtubule dynamics and limited actomyosin contractility, a property that generates the mechanical force required for changes in cell shape, which in turn can regulate cell adhesion and migration. Indeed, cells lacking FAM123A showed increased adhesion and decreased migration.

Citation: P. F. Siesser, M. Motolese, M. P. Walker, D. Goldfarb, K. Gewain, F. Yan, R. M. Kulikauskas, A. J. Chien, L. Wordeman, M. B. Major, FAM123A Binds to Microtubules and Inhibits the Guanine Nucleotide Exchange Factor ARHGEF2 to Decrease Actomyosin Contractility. Sci. Signal. 5, ra64 (2012).

Read the Full Text

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882