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

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Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration. / Xavier, Charles-Peter; Rastetter, Raphael H; Blömacher, Margit; Stumpf, Maria; Himmel, Mirko; Morgan, Reginald O; Fernandez, Maria-Pilar; Wang, Conan; Osman, Asiah; Miyata, Yoshihiko; Gjerset, Ruth A; Eichinger, Ludwig; Hofmann, Andreas; Linder, Stefan; Noegel, Angelika A; Clemen, Christoph S.

in: SCI REP-UK, Jahrgang 2, 2012, S. 241.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Xavier, C-P, Rastetter, RH, Blömacher, M, Stumpf, M, Himmel, M, Morgan, RO, Fernandez, M-P, Wang, C, Osman, A, Miyata, Y, Gjerset, RA, Eichinger, L, Hofmann, A, Linder, S, Noegel, AA & Clemen, CS 2012, 'Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration.', SCI REP-UK, Jg. 2, S. 241. https://doi.org/10.1038/srep00241

APA

Xavier, C-P., Rastetter, R. H., Blömacher, M., Stumpf, M., Himmel, M., Morgan, R. O., Fernandez, M-P., Wang, C., Osman, A., Miyata, Y., Gjerset, R. A., Eichinger, L., Hofmann, A., Linder, S., Noegel, A. A., & Clemen, C. S. (2012). Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration. SCI REP-UK, 2, 241. https://doi.org/10.1038/srep00241

Vancouver

Xavier C-P, Rastetter RH, Blömacher M, Stumpf M, Himmel M, Morgan RO et al. Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration. SCI REP-UK. 2012;2:241. https://doi.org/10.1038/srep00241

Bibtex

@article{ea13893247ef4810bf9e69c65107a1e6,
title = "Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration.",
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 the local morphology of complex actin structures and thereby inhibits cell migration.",
author = "Charles-Peter Xavier and Rastetter, {Raphael H} and Margit Bl{\"o}macher and Maria Stumpf and Mirko Himmel and Morgan, {Reginald O} and Maria-Pilar Fernandez and Conan Wang and Asiah Osman and Yoshihiko Miyata and Gjerset, {Ruth A} and Ludwig Eichinger and Andreas Hofmann and Stefan Linder and Noegel, {Angelika A} and Clemen, {Christoph S}",
year = "2012",
doi = "10.1038/srep00241",
language = "English",
volume = "2",
pages = "241",
journal = "SCI REP-UK",
issn = "2045-2322",
publisher = "NATURE PUBLISHING GROUP",

}

RIS

TY - JOUR

T1 - Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration.

AU - Xavier, Charles-Peter

AU - Rastetter, Raphael H

AU - Blömacher, Margit

AU - Stumpf, Maria

AU - Himmel, Mirko

AU - Morgan, Reginald O

AU - Fernandez, Maria-Pilar

AU - Wang, Conan

AU - Osman, Asiah

AU - Miyata, Yoshihiko

AU - Gjerset, Ruth A

AU - Eichinger, Ludwig

AU - Hofmann, Andreas

AU - Linder, Stefan

AU - Noegel, Angelika A

AU - Clemen, Christoph S

PY - 2012

Y1 - 2012

N2 - 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 the local morphology of complex actin structures and thereby inhibits cell migration.

AB - 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 the local morphology of complex actin structures and thereby inhibits cell migration.

U2 - 10.1038/srep00241

DO - 10.1038/srep00241

M3 - SCORING: Journal article

VL - 2

SP - 241

JO - SCI REP-UK

JF - SCI REP-UK

SN - 2045-2322

ER -