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- W2083716173 abstract "Casein kinase I (CKI) are a family of conserved second messenger-independent serine/threonine protein kinases found in all eukaryotes. 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. Here we report the isolation of cDNAs encoding human CKIαL and CKIαS. We find human CKIαL has a preference to phosphorylate phosvitin over casein, with a higher Km for casein than phosvitin, the reverse being the case for human CKIαS. Both human CKIαL, and CKIαS are derived from 4.2-kb mRNA transcripts and 2.4-kb transcripts, the latter probably generated by use of an alternate polyadenylation signal identified in the longer transcripts. The 4.2-kb transcripts contain six RNA-destabilising AU-rich element (ARE) motifs in the 3′-untranslated region (UTR), while the 2.4-kb transcripts contain a single ARE motif. 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. This is the first report of a kinase mRNA containing multiple RNA-destabilising AREs in the longer of two mRNA transcripts." @default.
- W2083716173 created "2016-06-24" @default.
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- W2083716173 date "2000-07-01" @default.
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- W2083716173 title "Human CKIαL and CKIαS are encoded by both 2.4- and 4.2-kb transcripts, the longer containing multiple RNA-destablising elements" @default.
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- W2083716173 doi "https://doi.org/10.1016/s0167-4781(00)00146-9" @default.
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