Corpus ID: 30891177

Phosphorylation of the beta subunit of casein kinase II in human A431 cells. Identification of the autophosphorylation site and a site phosphorylated by p34cdc2.

@article{Litchfield1991PhosphorylationOT,
  title={Phosphorylation of the beta subunit of casein kinase II in human A431 cells. Identification of the autophosphorylation site and a site phosphorylated by p34cdc2.},
  author={David W. Litchfield and Fred J. Lozeman and M F Cicirelli and M Harrylock and Lowell H. Ericsson and C Piening and Edwin G. Krebs},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 30},
  pages={
          20380-9
        }
}
  • David W. Litchfield, Fred J. Lozeman, +4 authors Edwin G. Krebs
  • Published in
    The Journal of biological…
    1991
  • Biology, Medicine
  • To examine the phosphorylation of casein kinase II in cells, the enzyme was isolated by immunoprecipitation from metabolically labeled human epidermal carcinoma A431 cells using polyclonal antipeptide antibodies specific for either the alpha subunit or the beta subunit of the enzyme. When isolated from 32P-labeled cells, the beta subunit was found to be significantly labeled on serine residues whereas only minimal labeling was associated with the alpha subunit. In vitro, the beta subunit of… CONTINUE READING

    Create an AI-powered research feed to stay up to date with new papers like this posted to ArXiv

    Citations

    Publications citing this paper.
    SHOWING 1-10 OF 45 CITATIONS

    Microtubule dependency of p34cdc2 inactivation and mitotic exit in mammalian cells

    VIEW 4 EXCERPTS
    CITES METHODS & BACKGROUND
    HIGHLY INFLUENCED

    Evidence for aggregation of protein kinase CK2 in the cell: a novel strategy for studying CK2 holoenzyme interaction by BRET2

    VIEW 14 EXCERPTS
    CITES BACKGROUND
    HIGHLY INFLUENCED

    Autophosphorylation at the regulatory β subunit reflects the supramolecular organization of protein kinase CK2

    VIEW 4 EXCERPTS
    CITES BACKGROUND
    HIGHLY INFLUENCED