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RP1 is a phosphorylation target of CK2 and is involved in cell adhesion

Frank Stenner1, Heike Liewen, Stephan Göttig

  • 1Division of Oncology, University Hospital Zurich, Zurich, Switzerland. stennerf@uhbs.ch

Plos One
|July 12, 2013
PubMed

Insights

Protein kinase CK2 phosphorylates RP1, a microtubule-binding protein, impacting cell adhesion. This phosphorylation event, particularly at Ser(236), influences N-cadherin levels and cell-endothelial interactions, suggesting a role in cancerogenesis.

Area of Science:

  • Cell Biology
  • Molecular Oncology
  • Biochemistry

Background:

  • RP1 (MAPRE2/EB2) is an EB1 family protein interacting with APC in the Wnt pathway, with its function less understood than other EB1 proteins.
  • RP1 has been recently linked to pancreatic cancerogenesis.
  • Protein kinase CK2 is frequently overexpressed in cancers, promoting proliferation and anti-apoptosis.

Purpose of the Study:

  • To investigate the interaction between protein kinase CK2 and RP1.
  • To determine if CK2 phosphorylates RP1 and the functional consequences of this phosphorylation on cell adhesion.

Main Methods:

  • In vitro kinase assays to assess CK2 phosphorylation of RP1.
  • Stable RP1 expression in cell lines to evaluate effects on N-cadherin and adhesion.
  • Use of a phospho-mimicking RP1 mutant (RP1-ASP(236)).
  • Analysis of cell adhesion under shear stress.
  • RP1 knockdown using shRNA.

Main Results:

  • CK2 phosphorylates RP1 at Ser(236) in vitro.
  • Stable RP1 expression leads to N-cadherin downregulation and impaired cell adhesion.
  • The RP1-ASP(236) mutant shows reduced adhesion to endothelial cells under shear stress.
  • Cells downregulate endogenous RP1 under shear stress to enhance adhesion.
  • RP1 suppression via shRNA significantly increases cell adherence.

Conclusions:

  • RP1 phosphorylation at Ser(236) by CK2 plays a significant role in regulating cell adhesion.
  • This interaction may offer new insights into the association between CK2 and EB1 family proteins in cancer biology.

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