title: Expanding roles of protein kinase CK2 in regulating plant growth and development.
abstract: Protein kinase CK2 (formerly known as casein kinase II) is a ubiquitious Ser/Thr kinase present in all eukaryotes. The α (catalytic) and β (regulatory) subunits of CK2 exist both as a tetrameric holoenzyme and as monomers in eukaryotic cells. CK2 has been implicated in multiple developmental and stress-responsive pathways including light signalling and circadian clock in plants. Recent studies using CK2 knockout and dominant negative mutants in Arabidopsis have uncovered new roles for this enzyme. CK2 substrates that have been identified so far are primarily transcription factors or regulatory proteins. CK2-mediated phosphorylation of these factors often results in alteration of the protein function including changes in the DNA-binding affinity, dimerization, stability, protein-protein interactions, and subcellular localization. CK2 has evolved as an essential housekeeping kinase in plants that modifies protein function in a dynamic way. This review summarizes the current knowledge of the role of CK2 in plant development.
authors.affiliation: Department of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.
authors.forename: Jidnyasa Jayant
authors.initials: JJ
authors.lastname: Mulekar
authors.affiliation: Department of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA huq@austin.utexas.edu.
authors.forename: Enamul
authors.initials: E
authors.lastname: Huq
mesh_terms: D047390:Casein Kinase II / Q000378:metabolism*; D057906:Circadian Clocks / Q000528:radiation effects; D008027:Light; D055537:Light Signal Transduction / Q000528:radiation effects; D008954:Models, Biological; D063245:Plant Development / Q000528:radiation effects; D010944:Plants / Q000201:enzymology*
chemical_list: D047390:Casein Kinase II
keywords: Circadian clock; flowering time; kinase; light signalling; phosphorylation.