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Published 23 October 2006. doi:10.1083/jcb.200608009
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 175, Number 2, 305-313
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Article

Phosphorylation and activity of the tumor suppressor Merlin and the ERM protein Moesin are coordinately regulated by the Slik kinase

Sarah C. Hughes1 and Richard G. Fehon2

1 Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada
2 Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637

Correspondence to Richard G. Fehon: rfehon{at}uchicago.edu

Merlin and Moesin are closely related members of the 4.1 Ezrin/Radixin/Moesin domain superfamily implicated in regulating proliferation and epithelial integrity, respectively. The activity of both proteins is regulated by head to tail folding that is controlled, in part, by phosphorylation. Few upstream regulators of these phosphorylation events are known. In this study, we demonstrate that in Drosophila melanogaster, Slik, a Ste20 kinase, controls subcellular localization and phosphorylation of Merlin, resulting in the coordinate but opposite regulation of Merlin and Moesin. These results suggest the existence of a novel mechanism for coordinate regulation of cell proliferation and epithelial integrity in developing tissues.

Abbreviations used in this paper: ERM, Ezrin/Radixin/Moesin; kd, kinase dead; MARCM, mosaic analysis with a repressible cell marker; PAK, p21-activated kinase; Thr, threonine; UAS, upstream activation sequence.


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