Synthesis of 3-aryl-9-chlorobenzo[e]-Δ<sup>3</sup>-indoline-2,8-diones

Carroll, F. Ivy; Blackwell, J. T.

doi:10.1039/c29690000925

Cited by 8 publications

(14 citation statements)

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“…The data in this paper show that p53 is a substrate for a kinase, CK-ll, whose activity increases in response to various mitogenic signals (Sommercom et al, 1987;Carroll et al, 1988;Klarlund and Czech, 1988;Ackermann and Osheroff, 1989;Carroll and Marshak, 1989). In one of these reports 3258 (Carroll and Marshak, 1989), 6-fold stimulations of CK-II activity were observed at 30 min, 12 h and 24 h after the addition of serum. p53 is also a growth-related protein, and its mRNA and protein levels rise significantly beginning at 6 h after serum stimulation and continue to rise throughout S phase (Reich and Levine, 1984).…”

Section: Discussionmentioning

confidence: 81%

“…The enzyme is activated by polyamines (Maenpaa, 1977), potently inhibited by heparin (Hathaway et al, 1980) and can utilize GTP as a phosphate donor. Considerable interest in CK-II has arisen recently because its activity is stimulated significantly in response to several mitogens including serum (Carroll and Marshak, 1989), TPA (Carroll et al, 1988), insulin (Sommercorn et al, 1987;Klarlund and Czech, 1988); insulin-like growth factor I (Klarlund and Czech, 1988) and epidermal growth factor (Sommercorn et al, 1987;Ackerman and Osheroff, 1989). Moreover, CK-II has a broad substrate specificity which includes nuclear oncoproteins such as Myc (Luscher et al, 1989), Myb (Krebs et al, 1988;Luscher et al, 1990), Fos (Carroll et al, 1988), the adenovirus ElA protein (Carroll et al, 1988), the human papillomavirus (types 6, 16 and 18) E7 protein (Firzlaff et al, 1989; Barbosa et al, 1990) and the SV40 large T antigen (Grasser et al, 1988;Krebs et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

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The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II.

et al. 1990

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The entire coding sequence of wild‐type mouse p53 was expressed in Escherichia coli under control of the PL promoter of bacteriophage lambda. The bacterial p53 protein had identical mobility to p53 from SV3T3 cells on SDS polyacrylamide gels and was recognized in bacterial lysates by three p53‐specific monoclonal antibodies, including PAb246 which is specific for wild‐type mouse p53. Immunoprecipitates of the bacterial p53 were phosphorylated by a highly purified preparation of rat casein kinase II; the stoichiometry of incorporation was approximately 1 mol of phosphate per mol of p53. The phosphorylated residue was identified by phosphopeptide mapping as serine 389, which is a major site of p53 phosphorylation in vivo. p53 (serine 389) kinase activity was detected on lysates of SV3T3 cells; this activity co‐purified with casein kinase II on phosphocellulose and Mono Q columns and was inhibited by heparin. Immunoprecipitates of the p53‐T antigen complex from SV3T3 cells also had associated serine 389 kinase activity. Phosphorylation of serine 389 by this kinase was potently inhibited by heparin and quenched by excess unlabelled GTP. The data indicate that p53 is a physiological substrate of casein kinase II, which is stimulated in response to mitogens, phosphorylates nuclear oncoproteins, and may play a role in the transduction of extracellular signals to the nucleus.

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Section: Discussionmentioning

confidence: 81%

Section: Introductionmentioning

confidence: 99%

The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II.

et al. 1990

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“…However, an effective peptide substrate for casein kinase II, DARPP95-107, (Kurihara et al, 1988;Girault et al, 1989) had no effect on the phosphorylation of APP645-695 when present in a 10-fold molar excess (data not shown). Furthermore, purified casein kinase II does not phosphorylate APP645-694 (T.Suzuki, unpublished observations) and the activity of casein kinase II is highest in the G1 phase of the cell cycle (Carroll and Marshak, 1989).…”

Section: Phosphorylation Of App Cytoplasmic Peptides In Vitro By Cdc2mentioning

confidence: 99%

Cell cycle-dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein.

et al. 1994

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Accumulation of the amyloid A beta peptide, which is derived from a larger precursor protein (APP), and the formation of plaques, are major events believed to be involved in the etiology of Alzheimer's disease. Abnormal regulation of the metabolism of APP may contribute to the deposition of plaques. APP is an integral membrane protein containing several putative phosphorylation sites within its cytoplasmic domain. We report here that APP is phosphorylated at Thr668 by p34cdc2 protein kinase (cdc2 kinase) in vitro, and in a cell cycle‐dependent manner in vivo. At the G2/M phase of the cell cycle, when APP phosphorylation is maximal, the levels of mature APP (mAPP) and immature APP (imAPP) do not change significantly. However, imAPP is altered qualitatively. Furthermore, the level of the secreted extracellular N‐terminal domain (APPS) is decreased and that of the truncated intracellular C‐terminal fragment (APPCOOH) is increased. These findings suggest the possibility that phosphorylation‐dependent events occurring during the cell cycle affect the metabolism of APP. Alterations in these events might play a role in the pathogenesis of Alzheimer's disease.

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“…As casein kinase II is likely to be responsible for the N-terminal phosphorylation of SRF, c-fos transcription would be linked to the activation of this kinase. This could explain the response of the c-fos gene to serum, epidermal growth factor or insulin, as casein kinase II is apparently induced by the same agents (Sommercorn et al, 1987;Carroll and Marshak, 1989).…”

Section: Phosphorylation Sites On Srf Affect Its Dna Binding Propertiesmentioning

confidence: 99%

Identification of multiple SRF N-terminal phosphorylation sites affecting DNA binding properties.

et al. 1992

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Human serum response factor (SRF) bearing a histidine tag was expressed using vaccinia virus. The recombinant protein was purified and shown to be phosphorylated mainly in its N‐terminal part. The corresponding phosphorylation sites were mapped by microsequencing and also appear to be phosphorylated in endogenous serum response factor. Four phosphorylation sites are located on serines within amino acids 77–85, while another phosphorylation site has been identified at Ser103. Mutations that considerably reduced or abolished phosphorylation at amino acids 77–85 caused a decrease in binding to the c‐fos serum response element accompanied by markedly reduced association and dissociation rates. In contrast, replacing Ser103 by alanine decreased DNA binding activity without drastically affecting the on/off rates. The combination of abolishing phosphorylation at amino acids 77–85 and 103 displayed greatly reduced on/off rates of DNA binding, but the reduction of DNA binding activity was partially alleviated. None of these mutations affect either the ability to interact with p62TCF or stimulation of transcription in vitro. These findings imply possible roles for SRF phosphorylation in the regulation of c‐fos transcription.

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Synthesis of 3-aryl-9-chlorobenzo[e]-Δ³-indoline-2,8-diones

Cited by 8 publications

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The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II.

The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II.

Cell cycle-dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein.

Identification of multiple SRF N-terminal phosphorylation sites affecting DNA binding properties.

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Synthesis of 3-aryl-9-chlorobenzo[e]-Δ3-indoline-2,8-diones

Cited by 8 publications

References 0 publications

The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II.

The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II.

Cell cycle-dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein.

Identification of multiple SRF N-terminal phosphorylation sites affecting DNA binding properties.

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Product

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Synthesis of 3-aryl-9-chlorobenzo[e]-Δ³-indoline-2,8-diones