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CK-2, a Multifunctional Protein Kinase and its Role during Proliferation

  • B. Boldyreff
  • K. Wehr
  • R. Hecht
  • O.-G. Issinger
Conference paper
Part of the NATO ASI Series book series (volume 76)

Abstract

Casein kinase 2 (CK-2) is a second messenger-independent protein kinase consisting of two or three subunits which form a tetrameric complex, either αα′β2 or α2β2. The α subunits (mol. mass 44–46 kDa) represent the catalytic subunits of the enzyme, whereas the β subunit is non-catalytic with a molecular mass of 26 kDa. No specific modulator as for the cAMP-dependent protein kinase is known which can dissociate the subunits or regulate the enzyme. CK-2 is unique among the protein kinases in being able to use ATP as well as GTP as a phosphoryl donor. It phosphorylates preferentially serine or threonine residues surrounded by a cluster of acidic amino acid residues (XS/TXXEX).

Keywords

Colon Crypt Tetrameric Complex Acidic Amino Acid Residue Phosphoryl Donor Reconstituted Enzyme 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Springer-Verlag Berlin Heidelberg 1993

Authors and Affiliations

  • B. Boldyreff
    • 1
  • K. Wehr
    • 1
  • R. Hecht
    • 1
  • O.-G. Issinger
    • 1
  1. 1.Institut für HumangenetikUniversität des SaarlandesHomburgGermany

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