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doi: 10.1242/10.1242/jcs.00074
Commentary |
Department of Biological Chemistry, University of Padova, V.le G. Colombo, 3 35121 Padova, Italy and Venetian Institute for Molecular Medicine (VIMM), Via Orus 2, 23129 Padova, Italy
e-mail: lorenzo.pinna{at}unipd.it
CK2 is an extremely conserved pleiotropic protein kinase with a growing
list of more than 300 substrates, the majority of which are proteins
implicated in signal transduction, gene expression and other nuclear
functions. The CK2 phosphoacceptor sites are specified by multiple acidic
residues, with the one at position +3 relative to the target residue being of
crucial relevance. The CK2 holoenzyme is composed of two catalytic subunits
(
,
'
' or 
'), which
are essential for cell viability, and a dimer of two non-catalytic ß
subunits, whose precise function is still poorly understood. Although the
ß subunits deeply affect many properties of CK2, both the isolated
catalytic subunits and the holoenzyme are constitutively active, which is
probably responsible for the oncogenic potential of CK2. Given the structure
of the holoenzyme, the ß subunits could undergo reversible dissociation
under physiological conditions and play a role as anchoring elements and/or as
a docking platform for protein substrates and effectors. These unusual
features are likely to be instrumental in the involvement of CK2 in a number
of key biological functions, notably RNA synthesis, Wnt signaling,
ubiquitination and cell survival.
Key words: Protein kinase, Casein kinase 2, Protein phosphorylation, Signal transduction, Cell regulation, Neoplasia, Apoptosis
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