High impact information on CSNK1A1

• In contrast, C kinase inhibition actually potentiates the initial growth response to L1 or N-cadherin [1].
• These observations suggest that a C-kinase-independent phosphorylation of hsp28 may be an early event in the cellular action of tumor necrosis factor alpha [2].
• Thr(18) was phosphorylated in vitro by casein kinase (CK1); this process required the prior phosphorylation of Ser(15) [3].
• Induction of urokinase-type plasminogen activator (uPA) in response to either reagents activating cAMP-dependent protein kinase (cAMP-PK) or the calcium ion phospholipid-dependent kinase (C-kinase) was compared in the LLC-PK1 and T47D cell lines [4].
• A second protein kinase CK1-mediated step negatively regulates Wnt signalling by disrupting the lymphocyte enhancer factor-1/beta-catenin complex [5].

Biological context of CSNK1A1

• Our data show that the latter in vivo phosphorylation is also at least partially due to CK-1 [6].
• The derived amino acid sequence of the human CK1 alpha is identical to the bovine counterpart except that it contains 12 extra amino acids at the carboxyl end [7].
• These YACs have been used for fluorescent in situ hybridization in order to localize the human CK1 alpha gene to chromosome 13q13 [7].
• The avian and mammalian CKI alpha isoform has four splice variants differing in the presence or absence of 28 amino acids ('(L)' insertion) in the catalytic domain and/or 12 amino acids ('(S)' insertion) in the regulatory domain [8].
• In vitro analysis of CKI alpha 3'-UTR RNA sequences suggests that in HeLa cells, the longer 3'-UTR transcripts are likely to degrade approximately 13 times faster than the shorter 3'-UTR transcripts [8].

Anatomical context of CSNK1A1

• Phosphorylation of recombinant human spermidine/spermine N(1)-acetyltransferase by CK1 and modulation of its binding to mitochondria: a comparison with CK2 [9].
• The role of C-kinase in the activation of human polymorphonuclear leukocytes has been examined using H-7, a recently described C-kinase inhibitor [10].
• The human CK1 delta gene was mapped to chromosome 17q25.2-q25.3 by fluorescence in situ hybridization and polymerase chain reaction analysis of the human/rodent hybrid cell panels [11].
• We conclude that CsA does not affect the activation of either C-kinase or cAMPd PK in T cell tumor lines when activated by either fresh serum or when stimulated with chemical agents [12].
• The effect of various differentiation-inducers on the activity of Ca2+, phospholipid-dependent protein kinase (C-kinase) activity and endogenous protein phosphorylation by the kinase were examined in the extracts of HL-60 cells [13].

Associations of CSNK1A1 with chemical compounds

• The results show that H-7 differentially affects the PMN functional events of secretion and superoxide release and suggests that an H-7 inhibitable C-kinase is not involved in chemotactic peptide induced activation of PMN and may not regulate stimulus induced PMN degranulation [10].
• Protein kinase CK1 is a p53-threonine 18 kinase which requires prior phosphorylation of serine 15 [14].
• We found that in neutrophils, TNF by itself does not induce: (1) an influx of sodium, (2) an alteration in activity or translocation of the calcium and phospholipid dependent protein kinase (C-kinase), or (3) a release of arachidonic acid from preloaded cells [15].
• The calmodulin and C-kinase antagonists melittin, calmidazolium, N-(6-aminohexyl)-5-chloro-1-napthalenesulfonamide (W7), and trifluoperazine (TFP) also inhibit the activity of the human erythrocyte Ca2+-dependent protease, calpain I [16].
• The stimulating effect of IL-1 beta on iR-ET production was respectively inhibited by protein kinase C (C kinase) inhibitor (H-7), Ca-calmodulin inhibitor (W-7), cyclic AMP-dependent protein kinase (A kinase) inhibitor (H-8) and tyrosine kinase inhibitor (genistain) in a dose-dependent fashion [17].

Enzymatic interactions of CSNK1A1

• The present work evaluates the ability of the cAMP-independent Ser/Thr-protein kinase CK1 to phosphorylate SSAT [9].
• Here, we identify CK1 and CK2 as major kinases that directly bind to and phosphorylate LEF-1 inducing distinct, kinase-specific changes in the LEF-1/DNA complex [5].

Other interactions of CSNK1A1

• Consistent with these observations, CK1-dependent phosphorylation inhibits, whereas CK2 activates LEF-1/beta-catenin transcriptional activity in reporter gene assays [5].
• These data highlight an additional and physiologically important target residue for CK1 in p53 and suggest a potential mechanism by which sequential modification of a pivotal N-terminal residue in p53 may occur following stress-activated modification of serine 15 [14].
• Interestingly, phosphorylation of E-cadherin by CK1 or CK2 prevented the inhibition of beta-catenin binding by src phosphorylation [18].
• The enzyme termed nowadays protein kinase CK2 was first described in liver extracts (as a mixture with protein kinase CK1), using casein as artificial substrate, by Burnett and Kennedy (1954) [19].
• CK1 and CK2 were distinguished from each other at the end of the sixties, and during the seventies CK2 was purified to homogeneity in several laboratories and thoroughly characterized as far as its subunit structure (alpha 2 beta 2), site specificity, and in vitro responsiveness to various effectors were concerned [19].

Analytical, diagnostic and therapeutic context of CSNK1A1

• Using this cDNA sequence and PCR amplification, YAC genomic clones that contain this human CK1 alpha sequence have been isolated [7].

References