Phosphorylation of casein kinase II by p34cdc2 in vitro and at mitosis.

Litchfield, David W.; Lüscher, B; Lozeman, Fred J.; Eisenman, Robert N.; Krebs, Edwin G.

doi:10.1016/s0021-9258(19)49661-0

Cited by 132 publications

(13 citation statements)

References 59 publications

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“…We identified pSer-209 of the CK regulatory subunit as a target of CDKN3-CDC2. CK has been implicated in controlling multiple stages of cell division (Hériche et al, 1997;Litchfield et al, 1992;St-Denis and Litchfield, 2009). Therefore, we asked whether CK plays a role in the SAC.…”

Section: Identification Of Candidate Mitotic Effectors Of the Cdkn3-cdc2 Signaling Axismentioning

confidence: 99%

The tumor suppressor CDKN3 controls mitosis

Nalepa

Barnholtz‐Sloan

Enzor

et al. 2013

Journal of Cell Biology

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Section: Identification Of Candidate Mitotic Effectors Of the Cdkn3-cdc2 Signaling Axismentioning

confidence: 99%

The tumor suppressor CDKN3 controls mitosis

Nalepa

Barnholtz‐Sloan

Enzor

et al. 2013

Journal of Cell Biology

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“…Furthermore, this phosphorylation seemingly regulates CK2 activity as phosphomimetic mutations of these residues promote cell death by mitotic catastrophe, and phosphoablative mutations cause cell cycle arrest after significant spindle damage [50]. CK2β is also phosphorylated during mitosis by CDK1 at serine 209 [51][52][53].…”

Section: Protein-protein Interactionsmentioning

confidence: 99%

CK2 Regulation: Perspectives in 2021

Roffey

Litchfield

2021

Biomedicines

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The protein kinase CK2 (CK2) family encompasses a small number of acidophilic serine/threonine kinases that phosphorylate substrates involved in numerous biological processes including apoptosis, cell proliferation, and the DNA damage response. CK2 has also been implicated in many human malignancies and other disorders including Alzheimer′s and Parkinson’s diseases, and COVID-19. Interestingly, no single mechanism describes how CK2 is regulated, including activation by external proteins or domains, phosphorylation, or dimerization. Furthermore, the kinase has an elongated activation loop that locks the kinase into an active conformation, leading CK2 to be labelled a constitutively active kinase. This presents an interesting paradox that remains unanswered: how can a constitutively active kinase regulate biological processes that require careful control? Here, we highlight a selection of studies where CK2 activity is regulated at the substrate level, and discuss them based on the regulatory mechanism. Overall, this review describes numerous biological processes where CK2 activity is regulated, highlighting how a constitutively active kinase can still control numerous cellular activities. It is also evident that more research is required to fully elucidate the mechanisms that regulate CK2 and what causes aberrant CK2 signaling in disease.

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“…In vivo, phosphorylation of the a and 0 subunits has been observed in reticulocytes and in chicken bursal lymphoma BK3A cells arrested at mitosis (Litchfield et al, 1992). In human epidermal carcinoma A431 cells, phosphorylation of the 0 subunit is estimated in response to epidermal growth factor (Ackerman et al, 1990).…”

mentioning

confidence: 99%

“…Autophosphorylation of the a subunit is observed in vitro only in the presence of basic polypeptides such as polyarginine, polylysine, histone, and protamine Meggioetal., 1983). In addition, the a and 0 subunits are reported to be substrates for p34cdc2 in vitro (Litchfield et al, 1991(Litchfield et al, , 1992Mulner-Lorillon et al, 1990); Ser209 has been identified as the site of phosphorylation in the 0 subunit (Litchfield et al, 1991).…”

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confidence: 99%

Effects of Autophosphorylation on Casein Kinase II Activity: Evidence from Mutations in the .beta. Subunit

Lin¹,

Sheu²,

Traugh³

1994

Biochemistry

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Casein kinase II is a heterotetramer composed of two catalytic (alpha) and two regulatory (beta) subunits. To examine the effects of autophosphorylation of the beta subunit on enzyme activity, two mutants of the beta subunit from Drosophila were constructed in which either Ser4 or Ser2-4 was changed to alanine residues by oligonucleotide-directed mutagenesis and the proteins were expressed in Escherichia coli. The wild-type alpha and individual beta subunits present in inclusion bodies were renatured, and the biochemical properties of the reconstituted holoenzymes were examined. Analysis of autophosphorylation revealed that phosphate incorporation was about 0.8 mol/mol of beta subunit for the wild type and Ala4 mutant; Ser2 and Ser3 were the major sites of autophosphorylation with some phosphate in Ser4 as shown by Edman degradation. No autophosphorylation was observed with the Ala2-4 mutant. Substitution of alanine for serine residues at positions 4 or 2-4 of the beta subunits did not influence the reassociation of the alpha and beta subunits to form holoenzyme, or the function of the beta subunit in stimulating catalytic activity or in responding to basic compounds. To measure the effects of autophosphorylation on casein kinase II activity, the wild-type and mutant holoenzymes were preincubated in the presence and absence of ATP, and the rate of phosphorylation was measured with various substrates. In the absence of autophosphorylation, the wild-type, Ala4, and Ala2-4 forms of the holoenzyme displayed similar rates of phosphorylation of glycogen synthase. After preincubation with ATP, the rate of phosphorylation of glycogen synthase by the wild-type and Ala4 enzymes was inhibited by 30%.(ABSTRACT TRUNCATED AT 250 WORDS)

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Phosphorylation of casein kinase II by p34cdc2 in vitro and at mitosis.

Cited by 132 publications

References 59 publications

The tumor suppressor CDKN3 controls mitosis

The tumor suppressor CDKN3 controls mitosis

CK2 Regulation: Perspectives in 2021

Effects of Autophosphorylation on Casein Kinase II Activity: Evidence from Mutations in the .beta. Subunit

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