title: CK2 interacting proteins: emerging paradigms for CK2 regulation?
abstract: Protein kinase CK2 represents a small family of highly conserved protein kinases involved in a complex series of cellular events. Furthermore, CK2 has been localised to many discrete cellular sites and has an extensive and diverse array of substrates and interaction partners in cells. Despite considerable investigation, the precise mechanism(s) of regulation of CK2 in cells remains poorly understood. In consideration of the prospect that cells contain many distinct sub-populations of CK2 that are distinguished on the basis of localisation and/or interactions with other cellular components, one possibility is that there may be differential regulation of specific sub-populations of CK2. With this in mind, some of the individual sub-populations of CK2 may be regulated through particular protein-protein interactions that may play a role in recruiting CK2 into the vicinity of its substrates and/or modulating its ability to phosphorylate specific cellular targets. In this respect, here we examine two CK2-interacting proteins, namely Pin1 and CKIP-1 that have been shown to participate in the modulation of CK2 specificity or the subcellular localisation of CK2, respectively. One aspect of this work has been focused on the prospect that Pin1 interacts with CK2 in response to UV stimulation in a manner analogous to the phosphorylation-dependent interactions of CK2 that occur following the mitotic phosphorylation of CK2. A second aspect of this work involves an examination of the structural basis for interactions between CK2 and CKIP-1 with emphasis on a putative HIKE domain in CK2.
authors.affiliation: Department of Biochemistry, Siebens-Drake Research Institute, University of Western Ontario, London, Ontario, Canada N6A 5CI.
authors.forename: Mary Ellen K
authors.initials: ME
authors.lastname: Olsten
authors.forename: Jane E
authors.initials: JE
authors.lastname: Weber
authors.forename: David W
authors.initials: DW
authors.lastname: Litchfield
mesh_terms: D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000378:metabolism; D047390:Casein Kinase II / Q000378:metabolism / Q000502:physiology*; D045744:Cell Line, Tumor; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D019696:Peptidylprolyl Isomerase / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism; D014466:Ultraviolet Rays
chemical_list: D002352:Carrier Proteins; D047908:Intracellular Signaling Peptides and Proteins; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; C408877:PLEKHO1 protein, human; D016159:Tumor Suppressor Protein p53; D047390:Casein Kinase II; C000606846:PIN1 protein, human; D019696:Peptidylprolyl Isomerase