Specific Binding of Protein Kinase CK2 Catalytic Subunits to Tubulin

FEBS Lett. 1999 Nov 26;462(1-2):51-6. doi: 10.1016/s0014-5793(99)01492-1.

Abstract

Protein kinase CK2 is composed of two regulatory beta-subunits and two catalytic alpha- or alpha'-subunits. To analyse these subunits individually we generated antibodies against unique peptides derived from the alpha-, alpha'- and beta-subunit. Immunofluorescence studies with these antibodies revealed the presence of all three CK2 subunits in the cytoplasm and weakly in the nucleus with strong signals around the nuclear membrane. Double staining experiments revealed a co-localisation of all three subunits with tubulin. A direct association between the CK2 alpha- and the alpha'-subunit and tubulin was confirmed by co-immunoprecipitation experiments as well as by Far Western analysis. There was no binding of the CK2 beta-subunit to tubulin. Thus, with tubulin we have identified a new binding partner specific for the catalytic subunits of CK2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Casein Kinase II
  • Catalytic Domain
  • Cells, Cultured
  • Fluorescent Antibody Technique, Indirect
  • Mice
  • Precipitin Tests / methods
  • Protein Binding
  • Protein-Serine-Threonine Kinases / immunology
  • Protein-Serine-Threonine Kinases / metabolism*
  • Tubulin / metabolism*

Substances

  • Tubulin
  • Casein Kinase II
  • Protein-Serine-Threonine Kinases