Classification of Protein Kinases into Messenger-Dependent and Independent Kinases. The Regulation of Independent Kinases

Sommercorn, J; Krebs, Edwin G.

doi:10.1007/978-1-4684-9042-8_32

Cited by 5 publications

(5 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Activation of CKII could be one of several potential intermediate steps in transduction, or it may directly pass the signal to some target proteins. Consistent with the latter possibility is the fact that CKII phosphorylates a variety of key enzymes and proteins that contribute to the regulation of numerous cellular processes (12).…”

Section: Resultsmentioning

confidence: 89%

“…The function of the nuclear enzyme is not understood, but there is some evidence that it could contribute to the regulation of gene expression and of the cell cycle. CKII phosphorylates several nuclear proteins, including DNA topoisomerases 1 (32) and II (25) and RNA polymerases I and II (12), all of which contribute to the regulation of RNA synthesis. CKII also phosphorylates high mobility group protein 14, and the phosphate content of this site varies with the cell cycle (33).…”

Section: Resultsmentioning

confidence: 99%

“…Such studies have been facilitated, however, by the development of a specific peptide substrate for CKII (13) that was useful for estimating changes in kinase activity during differentiation of 3T3-L1 cells (14). Because CKII appears to phosphorylate an insulin-stimulated phosphorylation site and because it has been implicated in the regulation of a variety of fundamental cellular processes, we undertook studies of the short-term regulation of CKII activity and found that the kinase is rapidly activated by insulin (12). In this paper, we report in detail the characteristics of the response of CKII to insulin and that the kinase is also activated by epidermal growth factor.…”

mentioning

confidence: 95%

“…Although CKII has been implicated in the regulation of a wide variety of cellular processes, including the synthesis of glycogen, fatty acids, RNA, and protein (11,12), there have been few studies of its regulation. Such studies have been facilitated, however, by the development of a specific peptide substrate for CKII (13) that was useful for estimating changes in kinase activity during differentiation of 3T3-L1 cells (14).…”

mentioning

confidence: 99%

See 3 more Smart Citations

Activation of casein kinase II in response to insulin and to epidermal growth factor.

Sommercorn

Mulligan

Lozeman

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

279

101

View full text Add to dashboard Cite

Insulin treatment enhances casein kinase II (CKII) activity in 3T3-L1 mouse adipocytes and H4-IIE rat bepatoma cells, the magnitude of the activation varying from 30% to 150%. Activation of CKH was apparent after 5 min of exposure of 3T3-L1 cells to insulin, was maximal by 10 min, and persisted through 90 min. The insulin-stimulated activity was inhibited by low concentrations of heparin and was stimulated by spermine. Activation of CKII was effected by physiological concentrations of insulin'(EC50 = 0.15 nM), suggesting that the effect is a true insulin response and not one mediated through insulin-like growth factor receptors. Epidermal growth factor (100 ng/ml for 10 min) also activated CKII in A431 human carcinoma cells, which is consistent with other observations that insulin and epidermal growth factor may have some common effects. Insulin stimulation of CKII activity was due to an increase in the maximal velocity of the kinase; the apparent Km for peptide substrate was not altered. Enhanced activity did not appear to result from increased synthesis of CKII protein, because cycloheximide did not block the effect and because an immunoblot developed with antiserum to CKII showed no effect of insulin on the cytosolic'concentration of CKII. Because insulin-stimulated CKII activity was maintained after chromatography ofcell extracts on Sephadex G-25, it is unlikely that the effect is mediated by a low-molecularweight activator ofthe kinase. Rather, the results are consistent with the possibility that insulin activates CKII by promoting a covalent modification of the kinase.There is considerable evidence that reversible protein phosphorylation contributes to the mechanism of insulin action (reviewed in ref. 1). The f3 subunit of the insulin receptor is a protein-tyrosine kinase that is activated by insulin, and the hormone promotes phosphorylation of several proteins on tyrosine residues (1). Insulin also enhances phosphorylation of sefine and threonine residues in proteins, including the insulin receptor (1), ribosomal protein S6 (2-4), ATP-citrate lyase (5, 6), membrane-bound cAMP phosphodiesterase (7) Although CKII has been implicated in the regulation of a wide variety of cellular processes, including the synthesis of glycogen, fatty acids, RNA, and protein (11, 12), there have been few studies of its regulation. Such studies have been facilitated, however, by the development of a specific peptide substrate for CKII (13) that was useful for estimating changes in kinase activity during differentiation of 3T3-L1 cells (14). Because CKII appears to phosphorylate an insulin-stimulated phosphorylation site and because it has been implicated in the regulation of a variety of fundamental cellular processes, we undertook studies of the short-term regulation of CKII activity and found that the kinase is rapidly activated by insulin (12). In this paper, we report in detail the characteristics of the response of CKII to insulin and that the kinase is also activated by epidermal growth factor. EXPERIMENTAL PROCE...

show abstract

Section: Resultsmentioning

confidence: 89%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 95%

mentioning

confidence: 99%

See 2 more Smart Citations

Activation of casein kinase II in response to insulin and to epidermal growth factor.

Sommercorn

Mulligan

Lozeman

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

279

101

View full text Add to dashboard Cite

show abstract

“…Because of the universal reaction, catalyzed by PKA (phosphate transfer to proteins), which is catalyzed also by a number of other protein kinases (7,10,11,18), the specific histochemical demonstration of this enzyme by its chemical reaction seems to be impossible. The immunocytochemical method can overcome these difficulties.…”

Section: Discussionmentioning

confidence: 99%

Immunocytochemical demonstration of protein kinase A in the rat hippocampus.

Poeggel

Luppa

Brandt

et al. 1989

Acta Histochem. Cytochem

View full text Add to dashboard Cite

Regulation of protein phosphorylation in Dictyostelium discoideum

Anschutz

Tao

et al. 1991

Dev. Genet.

View full text Add to dashboard Cite

We have examined the phosphorylation of the cyclic adenosine 3':5' monophosphate (cAMP) cell surface chemotactic receptor and a 36 kDa membrane-associated protein (p36) in Dictyostelium discoideum. The activity of CAR-kinase, the enzyme responsible for the phosphorylation of the cAMP receptor, was studied in plasma membrane preparations. It was found that, as in intact cells, the receptor was rapidly phosphorylated in membranes incubated with [gamma 32P] adenosine triphosphate (ATP) but only in the presence of cAMP. This phosphorylation was not observed in membranes prepared from cells which did not display significant cAMP binding activity. cAMP could induce receptor phosphorylation at low concentrations, while cyclic guanosine 3':5' monophosphate (cGMP) could elicit receptor phosphorylation only at high concentrations. Neither ConA, Ca2+, or guanine nucleotides had an effect on CAR-kinase. It was also observed that 2-deoxy cAMP but not dibutyryl cAMP induced receptor phosphorylation. The data suggest that the ligand occupied form of the cAMP receptor is required for CAR-kinase activity. Although the receptor is rapidly dephosphorylated in vivo, we were unable to observe its dephosphorylation in vitro. In contrast, p36 was rapidly dephosphorylated. Also, unlike the cAMP receptor, the phosphorylation of p36 was found to be regulated by the addition of guanine nucleotides. Guanosine diphosphate (GDP) enhanced the phosphorylation while guanosine triphosphate (GTP) decreased the radiolabeling of p36 indicating that GTP can compete with ATP for the nucleotide triphosphate binding site of p36 kinase. Thus was verified using radiolabeled GTP as the phosphate donor. Competition experiments with GTP gamma S, ATP, GTP, CTP, and uridine triphosphate (UTP) indicated that the phosphate donor site of p36 kinase is relatively non-specific.(ABSTRACT TRUNCATED AT 250 WORDS)

show abstract

Classification of Protein Kinases into Messenger-Dependent and Independent Kinases. The Regulation of Independent Kinases

Cited by 5 publications

References 58 publications

Activation of casein kinase II in response to insulin and to epidermal growth factor.

Activation of casein kinase II in response to insulin and to epidermal growth factor.

Immunocytochemical demonstration of protein kinase A in the rat hippocampus.

Regulation of protein phosphorylation in Dictyostelium discoideum

Contact Info

Product

Resources

About