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Structure of protein kinase CK2: Dimerization of the human β‐subunit
Author(s) -
Boldyreff Brigitte,
Mietens Ulrike,
Issinger Olaf-Georg
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01497-7
Subject(s) - protein subunit , chemistry , microbiology and biotechnology , biochemistry , biology , gene
Protein kinase CK2 has been shown to be elevated in all so far investigated solid tumors and its catalytic subunit has been shown to serve as an oncogene product. CK2 is a hetero‐tetrameric serine‐threonine kinase composed of two catalytic (α and/or α′) and two regulatory β‐subunits. Using the two‐hybrid system we could show that the α‐ or α′‐subunits of CK2 can interact with the β‐subunits of CK2, but not with other α‐ or α′‐subunits. By comparison, the β‐subunit of CK2 can interact with another β‐subunit. Important amino acids for successful dimerization of the β‐subunit were localized between amino acid residues 156 and 165. Furthermore, we identified residues between amino acid 170 and 180 which antagonize the dimerization.