Abstract：
:CK2 is a serine/threonine kinase with many substrates, largely unknown modes of regulation and essential roles in mitotic progression. CK2α, a catalytic subunit of CK2, is phosphorylated in mitosis, and here we examine the effect of phosphorylation on CK2α localization. Using phosphospecific antibodies, we show that CK2α localizes to the mitotic spindle in a phosphorylation-dependent manner. Mitotic spindle localization requires the unique C-terminus of CK2α, and involves a novel regulatory mechanism in which phosphorylation of CK2α facilitates binding to the peptidyl-prolyl isomerase Pin1, which is required for CK2α mitotic spindle localization. This could explain how the constitutive activity of CK2α might be targeted towards mitotic substrates. Furthermore, because Pin1 has many important spindle substrates, this might represent a general mechanism for localization of mitotic signalling proteins.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
St-Denis NA,Bailey ML,Parker EL,Vilk G,Litchfield DWdoi
10.1242/jcs.077446subject
Has Abstractpub_date
2011-07-15 00:00:00pages
2341-8issue
Pt 14eissn
0021-9533issn
1477-9137pii
jcs.077446journal_volume
124pub_type
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