TY  - JOUR
A1  - Stenner, Frank
A1  - Liewen, Heike
A1  - Göttig, Stephan
A1  - Henschler, Reinhard
A1  - Markuly, Norbert
A1  - Kleber, Sascha
A1  - Faust, Michael
A1  - Mischo, Axel
A1  - Bauer, Stefan
A1  - Zweifel, Martin
A1  - Knuth, Alexander
A1  - Renner, Christoph
A1  - Wadle, Andreas
T1  - RP1 is a phosphorylation target of CK2 and is involved in cell adhesion
T2  - PLoS One
N2  - RP1 (synonym: MAPRE2, EB2) is a member of the microtubule binding EB1 protein family, which interacts with APC, a key regulatory molecule in the Wnt signalling pathway. While the other EB1 proteins are well characterized the cellular function and regulation of RP1 remain speculative to date. However, recently RP1 has been implicated in pancreatic cancerogenesis. CK2 is a pleiotropic kinase involved in adhesion, proliferation and anti-apoptosis. Overexpression of protein kinase CK2 is a hallmark of many cancers and supports the malignant phenotype of tumor cells. In this study we investigate the interaction of protein kinase CK2 with RP1 and demonstrate that CK2 phosphorylates RP1 at Ser236 in vitro. Stable RP1 expression in cell lines leads to a significant cleavage and down-regulation of N-cadherin and impaired adhesion. Cells expressing a Phospho-mimicking point mutant RP1-ASP236 show a marked decrease of adhesion to endothelial cells under shear stress. Inversely, we found that the cells under shear stress downregulate endogenous RP1, most likely to improve cellular adhesion. Accordingly, when RP1 expression is suppressed by shRNA, cells lacking RP1 display significantly increased cell adherence to surfaces. In summary, RP1 phosphorylation at Ser236 by CK2 seems to play a significant role in cell adhesion and might initiate new insights in the CK2 and EB1 family protein association.
Y1  - 2013
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/29449
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-294492
SN  - 1932-6203
N1  - Copyright: © 2013 Stenner et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
VL  - 8
IS  - (7):e67595
PB  - PLoS
CY  - Lawrence, Kan.
ER  -