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Am J Physiol Cell Physiol (April 10, 2002). doi:10.1152/ajpcell.00070.2002
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Articles in PresS, published online ahead of print April 10, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00070.2002
Submitted on February 15, 2002
Accepted on April 8, 2002

A Translated Alu-Sequence Determines Nuclear Localization of a Novel Splice Variant of the Catalytic Subunit of Casein Kinase 2

Philip Hilgard1, Tianmin Huang1, Allan W. Wolkoff1, and Richard J. Stockert1*

1 Medicine, Albert Einstein College of Medicine, Bronx, New York, USA

* To whom correspondence should be addressed. E-mail: stockert{at}aecom.yu.edu.

Casein Kinase 2 (CK2) is a tetrameric enzyme constitutively expressed in all eukaryotic tissues. The two known isoforms of the catalytic subunit, CK2{alpha} and CK2{alpha}', have been reported to have distinct tissue-dependent subcellular distributions. We recently described a third isoform of the catalytic subunit, designated CK2{alpha}", which is highly expressed in liver. Immunoblot analysis of HuH-7 human hepatoma cell fractions as well as immunofluorescent microscopy revealed that CK2{alpha}" was exclusively localized to the nucleus preferentially associated with the nuclear matrix. CK2{alpha} and CK2'{alpha} were found in nuclear, membrane and cytosolic compartments. Deletion of the carboxy terminal 32 amino acids from the CK2{alpha}" sequence resulted in release of the truncated GFP-fusion protein from the nuclear matrix and redistribution to both the nucleus and the cytoplasm. Demonstration that the carboxy terminus is necessary but not sufficient for nuclear retention indicates that the underlying mechanism of CK2{alpha}" nuclear localization is dependent upon the secondary structure of the holoenzyme directed by the carboxy terminal sequence.




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