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.


Sci. Signal., 30 June 2009
Vol. 2, Issue 77, p. ra32
[DOI: 10.1126/scisignal.2000135]

RESEARCH

Editor's Summary

From Adhesions to Lamellae
The tight junction protein ZO-1 (zonula occludens-1) is involved in cell-cell adhesion, whereas integrins containing the {alpha}5 integrin subunit mediate both cell-cell and cell-matrix adhesion. Alterations in the abundance of ZO-1 and {alpha}5 are correlated with increased invasiveness in lung cancer cells. Through biochemical, RNA interference, and imaging techniques, Tuomi et al. found that ZO-1 and {alpha}5 interacted at the leading edge of migrating lung cancer cells, where the complex promoted lamellae formation and motility. Protein kinase C{varepsilon} (PKC{varepsilon}) promoted the phosphorylation of ZO-1 at Ser168, which triggered the relocalization of ZO-1 from tight junctions to lamellae. The ZO-1–{alpha}5 complex was detected only in migrating cells in vitro and, intriguingly, was also present only in a subset of cells in metastatic lung tumors, suggesting that ZO-1 and {alpha}5 integrin may be involved in motility and invasion in vivo.

Citation: S. Tuomi, A. Mai, J. Nevo, J. O. Laine, V. Vilkki, T. J. Öhman, C. G. Gahmberg, P. J. Parker, J. Ivaska, PKC{varepsilon} Regulation of an {alpha}5 Integrin–ZO-1 Complex Controls Lamellae Formation in Migrating Cancer Cells. Sci. Signal. 2, ra32 (2009).

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