NDLI: CK2 interacting proteins: Emerging paradigms for CK2 regulation?

Content Provider	Springer Nature Link
Author	Olsten, Mary Ellen K. Weber, Jane E. Litchfield, David W.
Copyright Year	2005
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.
Starting Page	115
Ending Page	124
Page Count	10
File Format	PDF
ISSN	03008177
Journal	Molecular and Cellular Biochemistry
Volume Number	274
Issue Number	1-2
e-ISSN	15734919
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2005-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	CK2-interacting proteins CKIP-1 HIKE domain p53 Pin1 protein kinase CK2 protein–protein interactions regulation signal transduction Cardiology Medical Biochemistry Oncology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Clinical Biochemistry Molecular Biology

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