KIF5C: A new binding partner for protein kinase CK2 with a preference for the CK2alpha' subunit.
 

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11-18-08 08:37 AM
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KIF5C: A new binding partner for protein kinase CK2 with a preference for the CK2alpha' subunit.
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KIF5C: A new binding partner for protein kinase CK2 with a preference for the CK2alpha' subunit.

Cell Mol Life Sci. 2008 Nov 18;

Authors: Schäfer B, Götz C, Dudek J, Hessenauer A, Matti U, Montenarh M

Protein kinase CK2 is a highly conserved serine/threonine kinase that is ubiquitously expressed in eukaryotic cells. CK2 is a constitutively active tetrameric enzyme composed of two catalytic alpha and/or alpha'-subunits and two regulatory beta-subunits. There is increasing evidence that the individual subunits may have independent functions and that they are asymmetrically distributed inside the cell. To gain a better understanding of the functions of the individual subunits, we employed a yeast-two-hybrid screen with CK2alpha and CK2alpha'. We identified the motor neuron protein KIF5C as a new binding partner for CK2. The interaction found in the yeast-two-hybrid screen was confirmed by co-sedimentation analysis on a sucrose density gradient and by co-immunoprecipitation analysis. Pull-down experiments and surface plasmon resonance spectrometry revealed a direct binding of KIF5C to CK2alpha'. Co-localization studies with neuroblastoma cells, bone marrow and with primary neurons confirmed the biochemical analysis that KIF5C preferentially bound to CK2alpha'.

PMID: 19011756 [PubMed - as supplied by publisher]