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How druggable is protein kinase CK2?
Author(s) -
Cozza Giorgio,
Bortolato Andrea,
Moro Stefano
Publication year - 2010
Publication title -
medicinal research reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.868
H-Index - 130
eISSN - 1098-1128
pISSN - 0198-6325
DOI - 10.1002/med.20164
Subject(s) - druggability , kinase , protein kinase a , cytosol , biochemistry , protein subunit , phosphorylation , enzyme , biology , chemistry , microbiology and biotechnology , computational biology , gene
CK2 is a pleiotropic, ubiquitous, and constitutively active protein kinase (PK), with both cytosolic and nuclear localization in most mammalian cells. The holoenzyme is generally composed of two catalytic (α and/or α′) and two regulatory (β) subunits, but the free α/α′ subunits are catalytically active by themselves and can be present in cells under some circumstances. CK2 catalyzes the phosphorylation of more than 300 substrates characterized by multiple acidic residues surrounding the phosphor‐acceptor amino acid, and, consequently, it plays a key role in several physiological and pathological processes. But how can one kinase orchestrate all these tasks faithfully? How is it possible that one kinase can, despite all pleiotropic characteristics of PKs in general, be involved in so many different biochemical events? Is CK2 a druggable target? Several questions are still to be clearly answered, and this review is an occasion for a fruitful discussion. © 2009 Wiley Periodicals, Inc. Med Res Rev, 30, No. 3, 419–462, 2010