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  • Title: KIF5C: a new binding partner for protein kinase CK2 with a preference for the CK2alpha' subunit.
    Author: Schäfer B, Götz C, Dudek J, Hessenauer A, Matti U, Montenarh M.
    Journal: Cell Mol Life Sci; 2009 Jan; 66(2):339-49. PubMed ID: 19011756.
    Abstract:
    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'.
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