Journal
JOURNAL OF CELL SCIENCE
Volume 123, Issue 12, Pages 2057-2066Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.064550
Keywords
ERM proteins; Actin cytoskeleton; PtdIns(4,5)P-2; Moesin; Drosophila morphogenesis
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Funding
- ACI Biologie du Developpement et Physiologie Integrative [030023]
- ARC [3832, 1114]
- FRM [Equipe 2005]
- Canadian Institutes for Health Research [MOP-89877]
- Ministere de la Recherche
- Lavoisier fellowship
- Long Term EMBO fellowship
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The ezrin, radixin and moesin (ERM) proteins regulate cell membrane architecture in several cellular contexts. Current models propose that ERM activation requires a PtdIns(4,5)P-2-induced conformational change, followed by phosphorylation of a conserved threonine. However, how these inputs contribute in vivo to orchestrate ERM activation is poorly understood. We addressed this issue by evaluating the contribution of PtdIns(4,5)P-2 and phosphorylation to the regulation of moesin during Drosophila development. Unexpectedly, we found that a form of moesin that cannot be phosphorylated displayed significant activity and could substitute for the endogenous product during wing morphogenesis. By contrast, we also show that PtdIns(4,5)P-2 binding is essential for moesin recruitment to the membrane and for its subsequent phosphorylation. Our data indicate that PtdIns(4,5)P-2 acts as a dosing mechanism that locally regulates ERM membrane recruitment and activation, whereas cycles of phosphorylation and dephosphorylation further control their activity once they have reached the cell cortex.
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