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, Vol. 2, 2012, p. 241.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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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 -