Ezrin/moesin in motile Walker 256 carcinosarcoma cells: signal-dependent relocalization and role in migration

Rossy, Jérémie; Gutjahr, Marc C; Blaser, Nelsy; Schlicht, Dominique; Niggli, Verena (2007). Ezrin/moesin in motile Walker 256 carcinosarcoma cells: signal-dependent relocalization and role in migration. Experimental cell research, 313(6), pp. 1106-20. San Diego, Calif.: Elsevier 10.1016/j.yexcr.2006.12.023

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Rat Walker 256 carcinosarcoma cells spontaneously develop front-tail polarity and migrate in the absence of added stimuli. Constitutive activation of phosphatidylinositol-3 kinase (PI 3-kinase), Rac, Rho and Rho kinase are essential for these processes. Ezrin and moesin are putative targets of these signaling pathways leading to spontaneous migration. To test this hypothesis, we used specific siRNA probes that resulted in a downregulation of ezrin and moesin by about 70% and in a similar reduction in the fraction of migrating cells. Spontaneous polarization however was not affected, indicating a more subtle role of ezrin and moesin in migration. We provide furthermore evidence that endogenous ezrin and moesin colocalize with F-actin at the contracted tail of polarized cells, similar to ectopically expressed green fluorescent protein-tagged ezrin. Our results suggest that myosin light chain and ezrin are markers of front and tail, respectively, even in the absence of morphological polarization. We further show that endogenous ezrin and moesin are phosphorylated and that activities of PI-3 kinase, Rho and Rac, but not of Rho-kinase, are required for this C-terminal phosphorylation. Activation of protein kinase C in contrast suppressed phosphorylation of ezrin and moesin. Inhibition of ezrin phosphorylation prevented its membrane association.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Service Sector > Institute of Pathology

UniBE Contributor:

Rossy, Jérémie and Niggli, Verena

ISSN:

0014-4827

ISBN:

17292355

Publisher:

Elsevier

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:53

Last Modified:

04 May 2014 23:15

Publisher DOI:

10.1016/j.yexcr.2006.12.023

PubMed ID:

17292355

Web of Science ID:

000245412300004

URI:

https://boris.unibe.ch/id/eprint/22672 (FactScience: 35903)

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