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Gene Review

CSNK1A1L  -  casein kinase 1, alpha 1-like

Homo sapiens

Synonyms: CK1, CKI-alpha-like, Casein kinase I isoform alpha-like, MGC33182
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Disease relevance of CSNK1A1L

  • He also discusses his recent work on signal transduction pathways (hypoxia, nitric oxide, adenosine, and C kinase) in oxygen sensing and Epo gene expression [1].
  • We have examined phosphatidylinositol turnover and C-kinase distribution in a flat cellular ras-resistant cell line (C11) derived from Kirsten murine sarcoma virus (Ki-MSV) transformed NIH/3T3 cells (DT) [2].
  • The profile of cytokines induced by soluble leishmania antigen (SLA) and the Leishmania homologue of the mammalian receptor for activated C kinase (LACK), a candidate vaccine against leishmaniasis, and the cellular source of the cytokines produced in response to these antigens were analyzed in patients infected with Leishmania guyanensis [3].
  • This study reports the efficacy of a heterologous prime-boost vaccination using DNA and vaccinia viruses (Western Reserve [WR] virus and modified [attenuated] vaccinia virus Ankara [MVA]) expressing the LACK antigen (Leishmania homologue of receptors for activated C kinase) and an intradermal murine infection model employing Leishmania infantum [4].
  • Deregulation and/or the incidence of mutations in the coding sequence of CK1 isoforms have been linked to neurodegenerative diseases and cancer [5].

Psychiatry related information on CSNK1A1L

  • Candidate tau protein kinases include members of the casein kinase 1 (CK1) family of phosphotransferases, which are highly overexpressed in Alzheimer's disease brain and colocalize with neuritic and granulovacuolar lesions [6].

High impact information on CSNK1A1L

  • The state of phosphorylation of DARPP-32 at Thr34 depends on the phosphorylation state of two serine residues, Ser102 and Ser137, which are phosphorylated by CK2 and CK1, respectively [7].
  • Phosphorylation of Ser319 forms a consensus sequence for phosphorylation by CK1, allowing it to phosphorylate Ser322, which in turn primes the CK1-catalysed phosphorylation of Ser325 [8].
  • Four monoclonal antibodies designated CK1 - CK4 were obtained from fusions of mouse myeloma F0 cells with spleen cells from BALB/c mice immunized with cytoskeletal preparations made by treatment of human HeLa cells with non-ionic detergents [9].
  • These results suggest that activation of the C kinase by some agents is not sufficient for induction of HL-60 cell differentiation and imply that some of the biologic effects of phorbol esters may occur through a more complex mechanism than previously thought [10].
  • CK1 exists with NFAT1 in a high-molecular-weight complex in resting T cells but dissociates upon activation [11].

Chemical compound and disease context of CSNK1A1L

  • Stimulated motility of rheumatoid SF was inhibited by the pertussis toxin, staurosporine (C kinase inhibitor), and genistein (tyrosine kinase inhibitor), but not by A kinase inhibitor, H-8 [12].
  • CK1 alpha was expressed in Escherichia coli as a glutathione transferase fusion protein (GT-CK1 alpha) and certain of its characteristics were determined [13].

Biological context of CSNK1A1L

  • The CK1 docking motif is present in proteins of the Wnt, Hedgehog, and circadian-rhythm pathways, which also integrate the activities of CK1 and GSK3 [11].
  • CK1 phosphorylates only the SRR-1 motif, the primary region required for NFAT1 nuclear import [11].
  • A conserved DNA sequence element, termed cytokine 1 (CK-1), is found in the promoter regions of many hemopoietic growth factor (HGF) genes [14].
  • As both DiC8 and PMA stimulate the Ca2+- and phospholipid-dependent protein kinase (C-kinase) in vitro, the results support the hypothesis that the activation of C-kinase is a critical component of phorbol diester action on EGF receptor modulation and cell proliferation [15].
  • The CK-1 gene is present in all four salmonid species examined and the nucleotide sequences of the exons are highly conserved [16].

Anatomical context of CSNK1A1L

  • RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells [17].
  • Tumor-promoting phorbol esters have been found to bind and activate phospholipid/Ca2+-dependent or C-kinase, and several of their effects, including proliferative responses in lymphocytes, have been assumed to be related to activity of this enzyme [18].
  • At concentrations of soluble anti-T3 that partially activate T cells in the absence of macrophages, there was a 50 to 60% decrease in C-kinase activity in the cytosol, with a comparable increase in activity in the membrane fraction [19].
  • Protein kinase C-driven myristoylated alanine-rich C kinase substrate domain phosphorylation and intact zinc fingers are in turn essential for plasma membrane translocation [20].
  • Furthermore, levels of all CK1 isoforms are elevated in the CA1 region of AD hippocampus relative to controls, with one isoform, Ckidelta, being elevated >30-fold [21].

Associations of CSNK1A1L with chemical compounds

  • This was not seen with the putative C-kinase inhibitor, H-7 [22].
  • Antibody recognition and biochemical characteristics indicated that the 87-kDa phosphoprotein is the PKC substrate MARCKS (myristoylated, alanine-rich C-kinase substrate) [23].
  • These actions of novobiocin and butyrate were not mediated by the pathway of epidermal growth factor action or modulated by the diacylglycerol agonist 1-oleoyl-2-acetylglycerol and the C kinase inhibitor 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine [24].
  • R 59 022, a diacylglycerol kinase inhibitor. Its effect on diacylglycerol and thrombin-induced C kinase activation in the intact platelet [25].
  • Amino-acid residues that define the beta-chemokines of mammals are conserved in CK-1, including the paired cysteine motif, CC [16].

Analytical, diagnostic and therapeutic context of CSNK1A1L

  • Here we report the distribution of three CK1 isoforms (Ckialpha, Ckidelta, and Ckiepsilon) in AD and control brains using immunohistochemistry and Western analysis [21].
  • Following homogenization in Ca2+-free buffer, C-kinase can be separated from Ca2+/calmodulin-dependent protein kinase by centrifugation; C-kinase activity is found in the supernatant whereas essentially all of the Ca2+/calmodulin-dependent protein kinase is found in the membrane fraction [26].
  • Southern blotting with a 264-bp probe demonstrates that four or more fragments are obtained upon digestion of genomic DNA with EcoR1 and Hind3, suggesting that X. laevis possesses a family of related CK1 genes [13].
  • The presence of C-kinase isoforms in the E2 embryonic neural tissues has been probed on Western blots, revealing immunoreactivity for the atypical isoforms iota (or lambda) and zeta and the alpha, gamma, epsilon and mu isoforms [27].
  • Ca+2/phospholipid-dependent kinase (C-kinase) activity is intimately involved with the B-cell response after ligation of its mIg receptor [28].


  1. A quest for erythropoietin over nine decades. Fisher, J.W. Annu. Rev. Pharmacol. Toxicol. (1998) [Pubmed]
  2. Reduced protein kinase C activity in a ras-resistant cell line derived from Ki-MSV transformed cells. Kamata, T., Sullivan, N.F., Wooten, M.W. Oncogene (1987) [Pubmed]
  3. LACK-specific CD4(+) T cells that induce gamma interferon production in patients with localized cutaneous leishmaniasis during an early stage of infection. Bourreau, E., Prévot, G., Gardon, J., Pradinaud, R., Hasagewa, H., Milon, G., Launois, P. Infect. Immun. (2002) [Pubmed]
  4. Heterologous prime-boost vaccination with the LACK antigen protects against murine visceral leishmaniasis. Dondji, B., Pérez-Jimenez, E., Goldsmith-Pestana, K., Esteban, M., McMahon-Pratt, D. Infect. Immun. (2005) [Pubmed]
  5. The casein kinase 1 family: participation in multiple cellular processes in eukaryotes. Knippschild, U., Gocht, A., Wolff, S., Huber, N., Löhler, J., Stöter, M. Cell. Signal. (2005) [Pubmed]
  6. Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules. Li, G., Yin, H., Kuret, J. J. Biol. Chem. (2004) [Pubmed]
  7. DARPP-32: an integrator of neurotransmission. Svenningsson, P., Nishi, A., Fisone, G., Girault, J.A., Nairn, A.C., Greengard, P. Annu. Rev. Pharmacol. Toxicol. (2004) [Pubmed]
  8. Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion. Rena, G., Woods, Y.L., Prescott, A.R., Peggie, M., Unterman, T.G., Williams, M.R., Cohen, P. EMBO J. (2002) [Pubmed]
  9. Monoclonal cytokeratin antibodies that distinguish simple from stratified squamous epithelia: characterization on human tissues. Debus, E., Weber, K., Osborn, M. EMBO J. (1982) [Pubmed]
  10. Bryostatin, an activator of the calcium phospholipid-dependent protein kinase, blocks phorbol ester-induced differentiation of human promyelocytic leukemia cells HL-60. Kraft, A.S., Smith, J.B., Berkow, R.L. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  11. A conserved docking motif for CK1 binding controls the nuclear localization of NFAT1. Okamura, H., Garcia-Rodriguez, C., Martinson, H., Qin, J., Virshup, D.M., Rao, A. Mol. Cell. Biol. (2004) [Pubmed]
  12. Biochemical investigation of cell motile activity in rheumatoid synovial fluid. Takeuchi, K., Watanabe, H., Takagishi, K. J. Rheumatol. (1998) [Pubmed]
  13. The recombinant alpha isoform of protein kinase CK1 from Xenopus laevis can phosphorylate tyrosine in synthetic substrates. Pulgar, V., Tapia, C., Vignolo, P., Santos, J., Sunkel, C.E., Allende, C.C., Allende, J.E. Eur. J. Biochem. (1996) [Pubmed]
  14. A novel tumor necrosis factor-responsive transcription factor which recognizes a regulatory element in hemopoietic growth factor genes. Shannon, M.F., Pell, L.M., Lenardo, M.J., Kuczek, E.S., Occhiodoro, F.S., Dunn, S.M., Vadas, M.A. Mol. Cell. Biol. (1990) [Pubmed]
  15. sn-1,2-Dioctanoylglycerol. A cell-permeable diacylglycerol that mimics phorbol diester action on the epidermal growth factor receptor and mitogenesis. Davis, R.J., Ganong, B.R., Bell, R.M., Czech, M.P. J. Biol. Chem. (1985) [Pubmed]
  16. CK-1, a putative chemokine of rainbow trout (Oncorhynchus mykiss). Dixon, B., Shum, B., Adams, E.J., Magor, K.E., Hedrick, R.P., Muir, D.G., Parham, P. Immunol. Rev. (1998) [Pubmed]
  17. RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells. Chang, B.Y., Conroy, K.B., Machleder, E.M., Cartwright, C.A. Mol. Cell. Biol. (1998) [Pubmed]
  18. Phorbol ester induces tyrosine phosphorylation in normal and abnormal human B lymphocytes. Nel, A.E., Navailles, M., Rosberger, D.F., Landreth, G.E., Goldschmidt-Clermont, P.J., Baldwin, G.J., Galbraith, R.M. J. Immunol. (1985) [Pubmed]
  19. Reaction of T lymphocytes with anti-T3 induces translocation of C-kinase activity to the membrane and specific substrate phosphorylation. Nel, A.E., Bouic, P., Lattanze, G.R., Stevenson, H.C., Miller, P., Dirienzo, W., Stefanini, G.F., Galbraith, R.M. J. Immunol. (1987) [Pubmed]
  20. Dynamics of diacylglycerol kinase zeta translocation in living T-cells. Study of the structural domain requirements for translocation and activity. Santos, T., Carrasco, S., Jones, D.R., Mérida, I., Eguinoa, A. J. Biol. Chem. (2002) [Pubmed]
  21. A new molecular link between the fibrillar and granulovacuolar lesions of Alzheimer's disease. Ghoshal, N., Smiley, J.F., DeMaggio, A.J., Hoekstra, M.F., Cochran, E.J., Binder, L.I., Kuret, J. Am. J. Pathol. (1999) [Pubmed]
  22. Granulocyte-macrophage colony-stimulating factor induces a staurosporine inhibitable tyrosine phosphorylation of unique neutrophil proteins. Berkow, R.L. Blood (1992) [Pubmed]
  23. Glutamate-stimulated protein phosphorylation in cultured hippocampal pyramidal neurons. Scholz, W.K., Palfrey, H.C. J. Neurosci. (1991) [Pubmed]
  24. Alteration of differentiation state of human hepatocytes cultured with novobiocin and butyrate. Kaneko, Y., Nakayama, T., Tsukamoto, A., Kurokawa, K. Cancer Res. (1990) [Pubmed]
  25. R 59 022, a diacylglycerol kinase inhibitor. Its effect on diacylglycerol and thrombin-induced C kinase activation in the intact platelet. de Chaffoy de Courcelles, D.C., Roevens, P., Van Belle, H. J. Biol. Chem. (1985) [Pubmed]
  26. Ca2+/diacylglycerol-activated, phospholipid-dependent protein kinase in the Hermissenda CNS. Neary, J.T., Naito, S., De Weer, A., Alkon, D.L. J. Neurochem. (1986) [Pubmed]
  27. Induction of epithelio-mesenchymal transformation of quail embryonic neural cells by inhibition of atypical protein kinase-C. Minichiello, J., Ben-Ya'acov, A., Hearn, C.J., Needham, B., Newgreen, D.F. Cell Tissue Res. (1999) [Pubmed]
  28. C-kinase activity in normal B cells treated with Staphylococcus aureus, Cowan strain I, and phorbol ester: response differences in a patient with prolymphocytic leukaemia. Cooper, R., Louw, J., Daniels, J., de Beer, D.P., Nel, A.E. Immunology (1987) [Pubmed]
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