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Gene Review

CSNK1A1  -  casein kinase 1, alpha 1

Bos taurus

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High impact information on CSNK1A1

  • The CKI PCR product was used to probe a bovine brain cDNA library from which cDNAs corresponding to CKI (CKI-alpha) and two homologous enzymes (CKI-beta and CKI-gamma) were identified [1].
  • From these biochemical and immunological criteria it is concluded that the 82-kDa protein is the human neutrophil homolog of MARCKS, the myristoylated, alanine-rich C kinase substrate previously described in bovine and rat brain and in murine fibroblasts and macrophages [2].
  • These findings strongly suggest that C-kinase plays an important role in mediating tracheal smooth muscle contraction [3].
  • In addition, BAY K 8644 (20 nM), which has a minimal effect on tension by itself, could significantly enhance contraction induced by C-kinase activators [3].
  • In contrast, ionophores and C-kinase activators, in combination, acted synergistically to produce a prompt and sustained contractile response that is reminiscent of that observed in response to carbachol, a cholinergic agonist [3].

Biological context of CSNK1A1


Anatomical context of CSNK1A1

  • These data imply that the initial transient rise in the [Ca2+] of the cell cytosol plays a role in determining the extent to which C-kinase is shifted from its calcium-insensitive to its calcium-sensitive form [7].
  • Adrenal glomerulosa cells were shown to contain the calcium-activated, phospholipid-dependent protein kinase (C-kinase) [8].
  • Myristoylated alanine-rich C kinase substrates (MARCKS) is a prominent protein kinase C (PKC) substrate that is targeted to the plasma membrane by an aminoterminal myristoyl group [9].
  • A calcium phospholipid-dependent protein kinase (C-kinase) activity was detected in the soluble fraction of rod outer segments (ROS) of the bovine retina [10].
  • These results suggest that calcium, phospholipids and the C-kinase enzyme may play an important role in the functional regulation of rod photoreceptors and, with retinal, perhaps in the visual process as well [10].

Associations of CSNK1A1 with chemical compounds

  • The effects of divalent ionophores (A23187 and ionomycin), Ca2+ channel agonist (BAY K 8644), and protein kinase C (C-kinase) activators [phorbol 12-myristate 13-acetate (PMA), mezerein] on bovine tracheal smooth muscle contraction were investigated [3].
  • The present studies were undertaken to determine the respective roles of the two angiotensin II-induced changes in cellular calcium metabolism in modulating events during the sustained phase of cellular response which is thought to be mediated by the C-kinase branch of the calcium messenger system [7].
  • This actin was not phosphorylated by either cyclic AMP-dependent protein kinase or C kinase [11].
  • CK-3 (Mr 32,000) is readily separated from CK-2 by gel filtration and from CK-1 by hydroxyapatite chromatography [12].
  • The inhibition of CK-1 by heparin can be reversed by KCl (greater than 100 mM) [13].

Other interactions of CSNK1A1

  • Prephosphorylation of tau by A-kinase, C-kinase, or CK-2 (but not by CK-1, CaM kinase II or Gr kinase) increased both the rate and extent of a subsequent phosphorylation catalyzed by GSK-3 by several-fold [14].
  • Both GL and glycyrrhetinic acid (GA) at 100 microM significantly inhibited RNase activities of these two gbPs, both of which functioned as phosphate acceptors of C-kinase in vitro [15].


  1. Purification of casein kinase I and isolation of cDNAs encoding multiple casein kinase I-like enzymes. Rowles, J., Slaughter, C., Moomaw, C., Hsu, J., Cobb, M.H. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  2. Tumor necrosis factor alpha modifies agonist-dependent responses in human neutrophils by inducing the synthesis and myristoylation of a specific protein kinase C substrate. Thelen, M., Rosen, A., Nairn, A.C., Aderem, A. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  3. Activation of tracheal smooth muscle contraction: synergism between Ca2+ and activators of protein kinase C. Park, S., Rasmussen, H. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  4. Characterization of the phosphorylation sites in the chicken and bovine myristoylated alanine-rich C kinase substrate protein, a prominent cellular substrate for protein kinase C. Graff, J.M., Stumpo, D.J., Blackshear, P.J. J. Biol. Chem. (1989) [Pubmed]
  5. A novel, calcium-inhibitable casein kinase in Paramecium cells. Kissmehl, R., Treptau, T., Hauser, K., Plattner, H. FEBS Lett. (1997) [Pubmed]
  6. Effect of K252a, a protein kinase inhibitor, on the proliferation of vascular smooth muscle cells. Ohmi, K., Yamashita, S., Nonomura, Y. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  7. Role of calcium fluxes in the sustained phase of angiotensin II-mediated aldosterone secretion from adrenal glomerulosa cells. Kojima, I., Kojima, K., Rasmussen, H. J. Biol. Chem. (1985) [Pubmed]
  8. The temporal integration of the aldosterone secretory response to angiotensin occurs via two intracellular pathways. Kojima, I., Kojima, K., Kreutter, D., Rasmussen, H. J. Biol. Chem. (1984) [Pubmed]
  9. Thrombin-induced phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein in bovine pulmonary artery endothelial cells. Zhao, Y., Davis, H.W. J. Cell. Physiol. (1996) [Pubmed]
  10. Endogenous phosphorylation of retinal photoreceptor outer segment proteins by calcium phospholipid-dependent protein kinase. Kapoor, C.L., Chader, G.J. Biochem. Biophys. Res. Commun. (1984) [Pubmed]
  11. Preparation and characterization of bovine aortic actin. Cavadore, J.C., Axelrud-Cavadore, C., Berta, P., Harricane, M.C., Haiech, J. Biochem. J. (1985) [Pubmed]
  12. A new heparin-inhibited and polyamine-activated protein kinase from bovine kidney. Singh, T.J. FEBS Lett. (1989) [Pubmed]
  13. Inhibition of glycogen synthase (casein) kinase-1 by heparin. Singh, T.J. Arch. Biochem. Biophys. (1988) [Pubmed]
  14. Modulation of GSK-3-catalyzed phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases. Singh, T.J., Zaidi, T., Grundke-Iqbal, I., Iqbal, K. FEBS Lett. (1995) [Pubmed]
  15. Characterization of bovine angiogenin-1 and lactogenin-like protein as glycyrrhizin-binding proteins and their in vitro phosphorylation by C-kinase. Tanigawa, K., Fujihara, M., Sakamoto, R., Yanahira, S., Ohtsuki, K. Biol. Pharm. Bull. (2001) [Pubmed]
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