Cloning and chromosomal localization of the gene coding for human protein kinase CK1

Tapia, Claudio; Featherstone, T.; Gómez, Claudio; Taillon-Miller, Patricia; Allende, Catherine C.; Allende, Jorge E.

doi:10.1016/0014-5793(94)00679-2

Cited by 34 publications

(19 citation statements)

References 23 publications

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“…A 264-bp fragment was amplified and sequenced and found to correspond to a coding region of CK1. This fragment was also obtained from X. luevis genomic DNA and was very similar to the equivalent amplification product found in the isolation of CKI a from human DNA (Tapia et al, 1994). The PCR fragment was labeled with "P by random priming and the radioactive product was used as a probe to screen the same X .…”

Section: Methodsmentioning

confidence: 67%

“…A X. laevis CKI cDNA has been cloned and found to correspond to an a isoform that is identical to the human C K l a described by our laboratory (Tapia et al, 1994). The X. laevis CK1 a is also identical to the bovine CKI a, except for a carboxyl end segment of 1 2 amino acids not present in the bovine enzyme.…”

Section: Discussionmentioning

confidence: 73%

“…genes code for 3.5-37-kDa proteins, while the y and 6 genes are considerably larger. The human CKla (Tapia et al, 1994), CK16 and CKlc (Fish et al,199.5) have also been cloned, as have the rat y (three different genes) and 6 isoforms (Graves et al, 1993;Zhai et al, 1995).…”

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confidence: 99%

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The Recombinant α Isoform of Protein Kinase CK1 from Xenopus laevis can Phosphorylate Tyrosine in Synthetic Substrates

Pulgar

Tapia

Vignolo

et al. 1996

European Journal of Biochemistry

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The cDNA coding for protein kinase CKla has been cloned from a Xenopus laevis cDNA library.The derived amino acid sequence of the protein contains 337 amino acids and has a calculated molecular mass of 38 874 Da. The sequence is identical to that of the human CKla and to the bovine CKla, except that it is 12 amino acids longer than the latter protein. Southern blotting with a 264-bp probe demonstrates that four or more fragments are obtained upon digestion of genomic DNA with EcoRl and Hind3, suggesting that X. Zaevis possesses a family of related CK1 genes. CKla was expressed in Escherichia coli as a glutathione transferase fusion protein (GT-CKIa) and certain of its characteristics were determined. The recombinant GT-CKla fusion protein was found to have apparent K,,, values for ATP (12 pM), casein (1.5 mg/ml) and the specific peptide substrate RRKDLHDDEEDEAMSITA (180 pM) which are similar to those of the rat liver CK1 enzyme. The recombinant CKla activity is weakly inhibited by heparin, but strongly inhibited by poly(GI~*":Tyr~~). This inhibition is competitive and shows an approximate K, of .5 pM. CKla can phosphorylate the tyrosine residues of poly(ClusO:Tyr'") and the tyrosine residue in the synthetic peptide RRREEEYEEEE. This kinase preparation also autophosphorylates in serine, threonine and weakly in tyrosine.

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Section: Methodsmentioning

confidence: 67%

Section: Discussionmentioning

confidence: 73%

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The Recombinant α Isoform of Protein Kinase CK1 from Xenopus laevis can Phosphorylate Tyrosine in Synthetic Substrates

Pulgar

Tapia

Vignolo

et al. 1996

European Journal of Biochemistry

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“…Actually, our results indicate that the CK1 genes are differentially expressed during development. Although orthologous genes have been described in several different vertebrate species (Tapia et al, 1994;Zhang et al, 1996;Green and Bennet, 1998;Yong et al, 2000;Burzio et al, 2002), there are no comparative expression studies made during vertebrate development at the mRNA level. Several studies seeking to detect CK1 isoform protein in cell culture and adult tissues of different species have been carried out (Camacho et al, 2001;Kannanayakal, 2006).…”

Section: Discussionmentioning

confidence: 99%

The CK1 gene family: expression patterning in zebrafish development

Albornoz

Yáñez²,

Foerster

et al. 2007

Biol. Res.

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Protein kinase CK1 is a ser/thr protein kinase family which has been identified in the cytosol cell fraction, associated with membranes as well as in the nucleus. Several isoforms of this gene family have been described in various organisms: CK1α, CK1β, CK1δ, CK1ε and CK1γ. Over the last decade, several members of this family have been involved in development processes related to wnt and sonic hedgehog signalling pathways. However, there is no detailed temporal information on the CK1 family in embryonic stages, even though orthologous genes have been described in several different vertebrate species. In this study, we describe for the first time the cloning and detailed expression pattern of five CK1 zebrafish genes. Sequence analysis revealed that zebrafish CK1 proteins are highly homologous to other vertebrate orthologues. Zebrafish CK1 genes are expressed throughout development in common and different territories. All the genes studied in development show maternal and zygotic expression with the exception of CK1ε. This last gene presents only a zygotic component of expression. In early stages of development CK1 genes are ubiquitously expressed with the exception of CK1ε. In later stages the five CK1 genes are expressed in the brain but not in the same way. This observation probably implicates the CK1 family genes in different and also in redundant functions. This is the first time that a detailed comparison of the expression of CK1 family genes is directly assessed in a vertebrate system throughout development.

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“…Additional CKI genes have been isolated from other organisms, including the yeasts Sckizosacckaromyces pombe (Kearney et al, 1994;Wang et al, 1994) and Klyuveromyces lactis (M. Wesolowski-Louvel, unpublished data), Caenorhabditis elegans (Wilson et al, 1994), and humans (Tapia et al, 1994).…”

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confidence: 99%

Multiple Isoforms of Arabidopsis Casein Kinase I Combine Conserved Catalytic Domains with Variable Carboxyl-Terminal Extensions

et al. 1995

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Three cDNA clones encoding isoforms of casein kinase I (CKI) were isolated from Arabidopsis fhaliana. One full-length clone, designated CKI7, contained an open reading frame of 1371 bp encoding a protein of 51,949 D with an isoelectric point of 9.7. In addition to the highly conserved catalytic domain (of about 300 amino acids), the Arabidopsis CKI isoforms contain 150 to 180 amino acid carboxyl-terminal extensions, which show among themselves a lower leve1 of sequence conservation. These extensions do not show any sequence similarity to nonplant CKI isoforms, such as rat testis CK16, which is their closest isolated homolog, or to yeast CKI isoforms. Three additional isoforms of Arabidopsis CKI were found in the data bases of expressed sequence tags and/or were isolated serendipitously in nonspecific screening procedures by others. One of them also shows a carboxyl-terminal extension, but of only 80 amino acids. Casein kinase activity was detected in the soluble fraction of Escherichia coli strains expressing the CKll protein. This activity showed the crucial properties of CKI, including the ability to phosphorylate the D4 peptide, a specific substrate of CKI, and inhibition by K(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide, a specific CKI inhibitor. Like severa1 recombinant CKI isoforms from yeast, CKll was able to phosphorylate tyrosinecontaining acidic polymers.

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Cloning and chromosomal localization of the gene coding for human protein kinase CK1

Cited by 34 publications

References 23 publications

The Recombinant α Isoform of Protein Kinase CK1 from Xenopus laevis can Phosphorylate Tyrosine in Synthetic Substrates

The Recombinant α Isoform of Protein Kinase CK1 from Xenopus laevis can Phosphorylate Tyrosine in Synthetic Substrates

The CK1 gene family: expression patterning in zebrafish development

Multiple Isoforms of Arabidopsis Casein Kinase I Combine Conserved Catalytic Domains with Variable Carboxyl-Terminal Extensions

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