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First published online June 18, 2008
doi: 10.1242/10.1242/jcs.028415

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Tyrosine phosphorylation of annexin A2 regulates Rho-mediated actin rearrangement and cell adhesion

Ursula Rescher^1,*,, Carsten Ludwig^1,*, Vera Konietzko^1,*, Alexei Kharitonenkov² and Volker Gerke^1,

¹ Institute of Medical Biochemistry, Centre for Molecular Biology of Inflammation, and Interdisciplinary Clinical Research Centre, University of Muenster, 48149 Muenster, Germany
² Biotechnology Discovery Research, Lilly Research Laboratories, Indianapolis, IN 46285, USA

Authors for correspondence (e-mails: rescher{at}uni-muenster.de; gerke{at}uni-muenster.de)

Accepted 9 April 2008

Cell adhesion and motility require a dynamic remodelling of the membrane-associated actin cytoskeleton in response to extracellular stimuli that are primarily transmitted through receptor tyrosine kinases. In a cellular model system for tyrosine phosphorylation-based growth factor signaling, we observed that annexin A2 is tyrosine-phosphorylated upon insulin receptor activation. The phosphorylation precedes peripheral actin accumulations and subsequent cell detachment. These morphological changes are inhibited by annexin A2 depletion and require Rho/ROCK signaling downstream of tyrosine-phosphorylated annexin A2. A phospho-mimicking annexin A2 mutant is sufficient to drive peripheral actin accumulation and the resulting cell detachment in the absence of insulin stimulation. Thus, a tyrosine phosphorylation switch in annexin A2 is an important event in triggering Rho/ROCK-dependent and actin-mediated changes in cell morphology associated with the control of cell adhesion.

Key words: Adhesion, Actin cytoskeleton, Rho GTPases, Annexin A2, Tyrosine phosphorylation

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