The effect of serum, EGF, PGF2α and insulin on S6 phosphorylation and the initiation of protein and DNA synthesis

Thomas, George; Martı́n-Pérez, Jorge; Siegmann, Michel; Otto, Angela M.

doi:10.1016/0092-8674(82)90029-0

Cited by 356 publications

(161 citation statements)

References 37 publications

Supporting

Mentioning

150

Contrasting

Order By: Relevance

“…This result is in agreement with previous observations of PMA stimulation of tyrosine kinase activity [31,32]. A corollary to this is that the tumor-promoting abilities of phorbol esters may involve the activation of tyrosine kinase systems by PK-C. We believe our findings are consistent with previous reports of interkinase regulation [33,34] and strongly implicate such kinase 'cross-talk' in the IL3 signal transduction pathway.…”

Section: Discussionsupporting

confidence: 93%

Interleukin 3 and phorbol ester stimulate tyrosine phosphorylation of overlapping substrate proteins

Ferris

Willette-Brown

Martensen³

et al. 1989

FEBS Letters

View full text Add to dashboard Cite

FDC-PI is a murine myeloid cell line that requires interleukin 3 (IL3) for survival and proliferation. While the biological effects of IL3 have been well described, the biochemical mechanisms of IL3 actions have only recently been examined. We have investigated whether IL3 or PMA stimulates phosphorylation of proteins on tyrosine as well as on serine/threonine residues as previously described [(1986) Blood 68, 906-913; (1987) Biochem. J. 244, 683-691]. Here we report that both IL3 and PMA stimulate the tyrosine phosphorylation of at least two proteins: pp70 and pp50 in FDC-P1 cells.

show abstract

Section: Discussionsupporting

confidence: 93%

Interleukin 3 and phorbol ester stimulate tyrosine phosphorylation of overlapping substrate proteins

Ferris

Willette-Brown

Martensen³

et al. 1989

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…Comparisons can be drawn with the 40S subunit protein S6, which is phosphorylated during periods of tissue regeneration, development, cell growth and transformation (Thomas, 1986, and references therein). This protein is also phosphorylated in response to various growth factors and purified tyrosinespecific protein kinases (Thomas et al, 1982;Wettenhall et al, 1982;Martin-Perez et al, 1984;Maller et al, 1985). Phosphorylated 40S subunits appear to be utilised more efficiently in the formation of initiation complexes (Duncan & McConkey, 1982).…”

Section: Discussionmentioning

confidence: 99%

A sequence previously identified as metastasis-related encodes an acidic ribosomal phosphoprotein, P2

Sharp

Elvin²,

Walker³

et al. 1990

Br J Cancer

View full text Add to dashboard Cite

Summary We have used a metastasis-related human cDNA isolated from a liver metastasis from a colonic adenocarcinoma to screen a human breast carcinoma cDNA library for homologous sequences. Nucleotide sequence analysis of positive clones revealed that the cDNA represents a ribosomal phosphoprotein, P2. The expression of P2 mRNA was significantly higher (Student's t test, one tail; P.0.01) in seven fibroadenomas than in seven carcinomas, with an average five-fold difference. This enhanced expression level of P2 mRNA in benign fibroadenomas compared with malignant carcinomas is contrary to that expected, based on earlier work with normal colonic mucosa, colorectal carcinoma and hepatic metastasis. The identification of gene transcripts which differ in abundance and correlate with the metastatic phenotype may be of considerable importance both as diagnostic aids and in defining the changes associated with tumour progression and metastasis at the molecular level. The possible role that ribosomal proteins may play in the progression of carcinoma of the breast is discussed.

show abstract

“…4). This increase in S6 phosphorylation is probably due to the dilution of cells in fresh media and serum prior to infection as already described [28]. This kinetic analysis of ribosomal protein phosphorylation was carried out several times.…”

Section: Kinetic Of Phosphorylation Of S2 and S13 After Vaccinia Virumentioning

confidence: 99%

Ribosomal protein phosphorylation in vivo and in vitro by vaccinia virus

Buendia

Person-Fernandez

Beaud

et al. 1987

European Journal of Biochemistry

View full text Add to dashboard Cite

Ribosomal protein phosphorylation was investigated in Ehrlich ascites tumor cells infected with vaccinia virus (Copenhagen strain). After 90 rnin of simultaneous infection and 32P-labelling, ribosomal proteins Sa, S2 and S13 appear specifically phosphorylated as well as Sb/La, P1 and S6, which are also phosphorylated in control cells. Sa is an acidic protein, whose phosphorylation has not been observed previously. A kinetic study showed that S2 is phosphorylated very rapidly within 10 min after the beginning of infection and it is complete 1 h later. The phosphorylation of S13 begins after a lag time of about 1 h and is completed after about 2.5 h of infection. Moreover only one phosphate is incorporated into S13 on a serine residue while up to four phosphates are incorporated into S2, the first on a serine and the three following on threonine residues. In vivo experiments, carried out in the presence of cycloheximide and cordycepin, suggest a viral origin for the kinase involved in the phosphorylation of S2 and S13. Moreover, in vitro experiments demonstrated that the kinase associated with the viral cores is capable of phosphorylating S2 on a serine residue only. In our cell/virus system, no significant difference in S6 phosphorylation was detected, when compared to uninfected cells. It is concluded that the specific and efficient phosphorylation of three ribosomal proteins from the 40 S ribosomal subunit correlate well with possible translational mechanisms ensuring the efficient expression of early and late genes of vaccinia virus. In the light of these and previous results [Person, A. and Beaud, G. (1986) J. Biol. Chern. 261, 8283-82891, a mechanism is proposed for the shut-off of host protein synthesis and the selective translation of mRNAs of viral origin.Infection of cells with vaccinia virus, a DNA virus replicating in the cytoplasm [l], results in a shut-off of host protein synthesis concomittant to the translation of the viral early mRNAs transcribed from vaccinia cores. It was shown by Kaerlein and Horak that several ribosomal proteins of HeLa cells are modified after infection with vaccinia virus (WR strain) and they suggested a possible role of the phosphorylation of S2, S6 and S16 in the establishment of the shut-off of host protein synthesis [2, 31. These authors gave evidence that the protein kinase known to be associated with vaccinia virions [4-71 may play a role in the phosphorylation of the ribosomal proteins but an early virus-induced enzyme was also responsible for this effect [3].A protein-synthesis inhibitor, associated with vaccinia virions, has been recently purified yielding a 1 1-kDa basic protein [8]. This inhibitor is clearly different from vacciniaassociated protein kinase and is likely to be responsible for the shut-off of protein synthesis shown to occur in the absence of viral gene expression in several cell/vaccinia virus systems. Thus it has been supposed that, in a productive infection, a viral-coded protein is produced in sufficient amounts to re-

show abstract

The effect of serum, EGF, PGF2α and insulin on S6 phosphorylation and the initiation of protein and DNA synthesis

Cited by 356 publications

References 37 publications

Interleukin 3 and phorbol ester stimulate tyrosine phosphorylation of overlapping substrate proteins

Interleukin 3 and phorbol ester stimulate tyrosine phosphorylation of overlapping substrate proteins

A sequence previously identified as metastasis-related encodes an acidic ribosomal phosphoprotein, P2

Ribosomal protein phosphorylation in vivo and in vitro by vaccinia virus

Contact Info

Product

Resources

About