Journal article

Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration

Charles-Peter Xavier, Raphael H Rastetter, Margit Bloemacher, Maria Stumpf, Mirko Himmel, Reginald O Morgan, Maria-Pilar Fernandez, Conan Wang, Asiah Osman, Yoshihiko Miyata, Ruth A Gjerset, Ludwig Eichinger, Andreas Hofmann, Stefan Linder, Angelika A Noegel, Christoph S Clemen

Scientific Reports | NATURE PUBLISHING GROUP | Published : 2012

Abstract

CRN2 (synonyms: coronin 1C, coronin 3) functions in the re-organization of the actin network and is implicated in cellular processes like protrusion formation, secretion, migration and invasion. We demonstrate that CRN2 is a binding partner and substrate of protein kinase CK2, which phosphorylates CRN2 at S463 in its C-terminal coiled coil domain. Phosphomimetic S463D CRN2 loses the wild-type CRN2 ability to inhibit actin polymerization, to bundle F-actin, and to bind to the Arp2/3 complex. As a consequence, S463D mutant CRN2 changes the morphology of the F-actin network in the front of lamellipodia. Our data imply that CK2-dependent phosphorylation of CRN2 is involved in the modulation of t..

View full abstract

University of Melbourne Researchers

Grants

Awarded by German Research Foundation


Awarded by Spanish Ministry of Science and Innovation (MICINN)


Awarded by NATIONAL CANCER INSTITUTE


Awarded by Grants-in-Aid for Scientific Research


Funding Acknowledgements

CK2 alpha expression plasmids were generously provided by Drs. Odile Filhol-Cochet and Yves Goldberg (University Joseph Fourier, Grenoble, France), recombinant WH2 domain from CAP2 by Dr. Vivek Peche (University of Cologne, Cologne, Germany). We are grateful to Kevin Jack (University of Queensland, St. Lucia, Australia) for assistance with data acquisition on the in-house SAXS instrument. We thank Dr. Lorenzo A. Pinna (University of Padua, Padua, Italy) for helpful discussions. This work was supported by grants of the German Research Foundation awarded to C. S. C and A. A. N. (DFG: NO 113/22-1 and CL 381/2-1). Grant BFU2007-67876 support for R. O. M. and M. P. F. came from the Spanish Ministry of Science and Innovation (MICINN).