Oncogenes and signal transduction

Cantley, Lewis C.; Auger, Kurt R.; Carpenter, Christopher L.; Duckworth, Brian; Graziani, Andrea; Kapeller, Rosana; Soltoff, Stephen P.

doi:10.1016/0092-8674(91)90639-g

Cited by 2,721 publications

(1,497 citation statements)

References 190 publications

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“…This cascade increases the phosphorylation of c-Jun, an important component of AP-1 (Dong et al, 1994a, b;Angel and Karin et al, 1991). Since c-Src and Ha-Ras are primarily associated with the plasma membrane (Cantley et al, 1991), it was proposed that the signaling cascade leading to the c Figure 3 UVC-induced AP-1 activity in B82L, B82 and B82M721 cells. 5610 3 cells from di erent AP-1 reporter stable transfectants (as indicated) were seeded into each well of 96-well plates.…”

Section: Discussionmentioning

confidence: 99%

Signal transduction through atypical PKCs, but not the EGF receptor, is necessary for UVC-induced AP-1 activation in immortal murine cells

Huang

Dong

1997

Oncogene

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The exposure of mammalian cells to ultraviolet (u.v.) irradiation leads to activation of transcription factors, such as AP-1 and NFkB. It is postulated that the EGF receptor but not protein kinase C (PKC) is the major membrane mediator in UVC-induced signal transduction. We demonstrate here that the antisense oligonucleotides of PKCz and the dominant negative mutant of PKCl/i as well as dominant negative PKCz markedly blocked UVC-induced AP-1 activity. In contrast, UVC-induced AP-1 activity in cells devoid of the EGF receptor (B82), is not signi®cantly di erent from that of the stable transfectants with a kinase-de®cient EGF receptor (B82M721), or wild-type EGF receptor (B82L). This was found at all UVC irradiation doses and time courses studied, while high levels of EGF-induced AP-1 activity were observed in B82L cells but not in B82 cells. This evidence strongly suggests that atypical PKCs, but not the EGF receptor, is necessary for UVC-induced AP-1 activation in JB6 and B82 cells.

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Section: Discussionmentioning

confidence: 99%

Signal transduction through atypical PKCs, but not the EGF receptor, is necessary for UVC-induced AP-1 activation in immortal murine cells

Huang

Dong

1997

Oncogene

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“…All of these tyrosines lie within the consensus sequence YxxM (where x can be a wide range of possible residues). This motif appears therefore to be important for PI 3-kinase binding (Cantley et al, 1991) and recent structural studies on the N-terminal SH2 domain of p85a provide a molecular basis for this specificity (Booker et al, 1992). Studies with the recombinant N-and C-terminal SH2 domains of p85a have shown that both are capable of binding to sequences containing YxxM motifs.…”

Section: Sh2 Domain-specific Binding Sitesmentioning

confidence: 99%

New insights into protein‐tyrosine kinase receptor signaling complexes

et al. 1993

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“…ErbB3 contains ®ve C-terminal sites in the p85 binding motif, which, when phosphorylated, recruit and activate p85 PI3 kinase (Solto et al, 1994). In cells lacking ErbB3, EGF signals to PI3 kinase through the molecule cbl (Solto and Cantley, 1996), which contains two tyrosine residues in the YXXM p85 binding motif (Cantley et al, 1991). Like ErbB3, cbl is phosphorylated on these tyrosine residues, leading to p85 binding and PI3 kinase activation.…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation and nuclear exclusion of the forkhead transcription factor FKHR after epidermal growth factor treatment in human breast cancer cells

et al. 2000

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Akt, when activated by IGF/insulin, can phosphorylate forkhead transcription factors. We undertook this study to determine whether epidermal growth factor (EGF) treatment could produce a signaling cascade resulting in phosphorylation of the forkhead transcription factor FKHR in a breast cancer cell line, MDA-MB-231. After establishing ErbB1, cbl, PI3 kinase and Akt were activated in EGF treated MDA-MB-231, we determined by immunoblot with FKHR antiserum that the electrophoretic mobility of FKHR was retarded after EGF treatment. This mobility retardation was reversible by treatment with alkaline phosphatase, and immunoblot with phospho-Ser 256 FKHR antibody further con®rmed phosphorylation on an Akt consensus site after EGF treatment. EGF stimulated FKHR phosphorylation was blocked by the PI3 kinase inhibitor LY294002, and the ErbB1 inhibitor AG1478. FKHR immunoblotting after puri®cation of nuclear and cytoplasmic proteins showed that EGF induced a simultaneous increase of FKHR in the cytoplasm and decrease in the nucleus. This ®nding was con®rmed by immuno¯uorescence staining. Treatment of cells with pharmacological inhibitors of PI3 kinase or ErbB1 blocked this e ect. Thus, these results demonstrate the phosphorylation and nuclear exclusion of FKHR after EGF treatment by a PI3 kinase dependent mechanism, and represent the ®rst report of growth factor regulation of endogenous FKHR localization Oncogene (2000) 19, 4574 ± 4581.

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Oncogenes and signal transduction

Cited by 2,721 publications

References 190 publications

Signal transduction through atypical PKCs, but not the EGF receptor, is necessary for UVC-induced AP-1 activation in immortal murine cells

Signal transduction through atypical PKCs, but not the EGF receptor, is necessary for UVC-induced AP-1 activation in immortal murine cells

New insights into protein‐tyrosine kinase receptor signaling complexes

Phosphorylation and nuclear exclusion of the forkhead transcription factor FKHR after epidermal growth factor treatment in human breast cancer cells

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