Phosphorylation of casein kinase II

Paleń, E; Traugh, Jolinda A.

doi:10.1021/bi00236a035

Cited by 47 publications

(36 citation statements)

References 31 publications

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“…Furthermore, as shown here, the isoelectric points of CKIIa and CKIIa' differ by more than pH 1, and their autophosphorylation behaviour is not identical ; while recombinant CKIIa' significantly incorporates phosphoryl groups when incubated in the presence of ATP, CKIIa does not. A similar observation had been reported for the subunits of CKII from rabbit reticulocytes (Palen and Traugh, 1991). The CKIIa' autophosphorylation appears, moreover, to occur as a specific function of CKII substrates and CKIIP.…”

Section: Phosphorylation Of Different Ckii Substratessupporting

confidence: 84%

Recombinant human casein kinase II

Bodenbach

Fauss

Robitzki

et al. 1994

European Journal of Biochemistry

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Human casein kinase I1 (CKII) is a ubiquitous and multipotential Ser/Thr kinase involved in the regulation of cell growth and differentiation. Biochemically, two characteristics are particularly notable; first, the tetrameric composition of two catalytic subunits ( a and/or a') and two regulatory subunits @); second, the autophosphorylation of the holoenzyme at the N-terminus of CKIIP, suspected to be involved in tuning of the kinase activity. Whether CKIIa and CKIIa' reconstitute comparably with CKIIP to form holoenzyme is unclear. For a systematic investigation, the complete set of recombinant CKII subunits and of autophosphorylation mutants of C H I P were expressed in Escherichiu coli and comparative reconstitutions carried out. At 1 : 1 molar ratio, CKIIP stimulated both catalytic subunits roughly fivefold with phosvitin as a substrate. The level of activity reached with both of the reconstituted CKII isoforms was of the same order of magnitude as that of holoenzyme isolated from human placenta. It was also similar to a recombinant a,p2 holoenzyme whose expression had been attained in E. coli with a bicistronic construct containing the coding regions of CKIIP and CKIIa in a tandem arrangement. Both Ser2 and Ser3 were identified as the autophosphorylation sites ; replacement of one of these with Ala by oligonucleotide-mediated site-directed mutagenesis influenced only the extent of CKIIP autophosphorylation, replacement of both resulted in a loss of autophosphorylation. Despite these differences, the stimulatory effect of all the CKIIP mutants was comparable both to each other and to that of wild-type CKIIP. This was also obtained when substrates other than phosvitin were employed such as tubulin, or upstream-binding factor (UBF). However, the degree of stimulation was substrate specific and ranged from 2-5-fold with no major differences between CKIIa and CKIIa' stimulation. Calmodulin phosphorylation by both CKIIa and CKIIa' was decreased similarly by CKIIP and the CKIIP mutants. Proteins such as CAMP-1-esponsive-element-binding protein (CREB), HPVl6 E7 or Jun were not phosphorylated by either catalytic subunit but became substrates of both in the presence of CKIIP or CKIIP mutants. The data suggest that CKIIa and CKIIa' form similar CKII holoenzymes and that the tuning of holoenzyme activity is independent of the autophosphorylation status of CKIIP.Casein kinase type I1 (CKII) is one of three protein kinases named for their ability to phosphorylate acidic proteins such as casein. These are the authentic, mammary-gland-specific Golgi-located casein kinase and two operationally defined ubiquitous kinases, the casein kinase type I (CKI) and CKII. While Golgi-located CK definitely phosphorylates casein in vivo, CKI and CKII do not; these phosphorylate a vast array of cellular proteins including key factors of cell Correspondence to W. Pyerin, Biochemical Cell Physiology,

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Section: Phosphorylation Of Different Ckii Substratessupporting

confidence: 84%

Recombinant human casein kinase II

Bodenbach

Fauss

Robitzki

et al. 1994

European Journal of Biochemistry

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“…Poly lysine had little or no effect on phosphorylation of wheat germ EF-I{3y by the CK II fraction from reticulocytes. 15 ) In addition, phosphorylation of lX-casein by CK 11-2 was about 50% inhibited by polylysine. From these results, the effects of polylysine on phosphorylation seem Wheat EF-IfJfJ'y was phosphorylated by CK lIs, CK 11-1 (A) and CK 11·2 (B), from Arabidopsis thaliana.…”

Section: Phosphorylation Of Wheat Ef-1f3f3'y By Ck IImentioning

confidence: 95%

Analysis of Phosphorylation of Wheat Elongation Factor 1β and β′ by Casein Kinase II

Matsumoto

Mizoguchi²,

Oizumi

et al. 1993

Bioscience, Biotechnology, and Biochemistry

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“…The deduced amino acid sequence of Dictyostelium casein kinase II a has strong homology with sequences of both (93), whereas autophosphorylation of the a subunit is reported to be much less than that of the 13 subunit in other species (1,27,30,43) unless polylysine is present (88).…”

Section: Er-------------------90mentioning

confidence: 97%

Molecular cloning of casein kinase II alpha subunit from Dictyostelium discoideum and its expression in the life cycle.

Kikkawa¹,

Mann²,

Firtel³

et al. 1992

Mol. Cell. Biol.

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A Dictyostelium discoideum cDNA encoding an a-type subunit of casein kinase If was isolated, and its cDNA was used to study developmental expression of casein kinase Hi during the Dictyostelium life cycle. The 1.3-kb cDNA insert contained an open reading frame of 337 amino acids (Mr 39,900 Casein kinase II is a ubiquitous protein-serine/threonine kinase in eukaryotic cells that catalyzes the phosphorylation of many protein substrates and has been regarded as a second-messenger-independent protein kinase (reviewed in references 27, 43, 82, and 109). When isolated from most species, this enzyme is composed of an a subunit (37 to 44 kDa) and a v subunit (24 to 28 kDa) and exists as an a212tetramer. The primary amino acid sequences of the a and 13 subunits of several species, which have been determined by molecular cloning and by direct protein sequence analysis, are well conserved among the species thus far studied (8,14,25,45,47,49,51,58,66,69,80,83,87,96,104,106). The a subunit contains a protein kinase domain that is homologous to the catalytic domain of other protein kinases (42), whereas the 13 subunit shows no significant homology Vv ith other proteins except the Drosophila melanogaster steijate gene products (67). The 1 subunit is presumed to regulate the catalytic activity (17), although the precise role of this subunit is not clear (59). There is some evidence that the 13 subunit stabilizes the a subunit, but it is not required for the catalytic activity of the a subunit (32,40,108 (80). In yeast cells, disruption of both a-subunit genes causes inviability, whereas disruption of either one of these genes alone has no detectable phenotype. This finding indicates that at least one of the a-type subunits is essential and that the two a-type subunits can complement one another in S. cerevisiae (87).Casein kinase II is detected in both the nucleus and the cytoplasm by fractionation experiments (43, 109). Immunolocalization studies have yielded somewhat conflicting results about the subcellular localization of casein kinase II (30,60,112). In one study, all three subunits were found to be predominantly nuclear under all conditions (60), whereas in the another study, the a and 13 subunits were found to be mainly cytoplasmic in interphase and the a' subunit was nuclear in G1 and cytoplasmic in S phase (112). In the third study, casein kinase II was found in the nucleus of growing cells but distributed in the nucleus and cytoplasm in quiescent cells (30). A role for casein kinase II in the nucleus is suggested by recent studies showing that a number of the nuclear proteins, such as c-Myc (72), Max (7), c-Myb (71), serum response factor (74, 79), c-Fos (12), c-Jun (64), DNA ligase (90), topoisomerase II (10), the p53 tumor suppressor protein (81), the adenovirus ElA protein (12), the human papillomavirus E7 protein (6,35), and the simian virus 40 large T antigen (41, 59), are phosphorylated by casein kinase II in vitro at physiological sites and that the DNA-binding activity of some of these nuclear proteins is regu...

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Phosphorylation of casein kinase II

Cited by 47 publications

References 31 publications

Recombinant human casein kinase II

Recombinant human casein kinase II

Analysis of Phosphorylation of Wheat Elongation Factor 1β and β′ by Casein Kinase II

Molecular cloning of casein kinase II alpha subunit from Dictyostelium discoideum and its expression in the life cycle.

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