The v-rel oncogene encodes a κB enhancer binding protein that inhibits NF-κB function

Ballard, Dean W.; Walker, William H.; Doerre, Stefan; Sista, Prakash; Molitor, Jerry A.; Dixon, Eric P.; Peffer, Nancy J.; Hannink, Mark; Greene, Warner C.

doi:10.1016/0092-8674(90)90146-6

Cited by 313 publications

(264 citation statements)

References 42 publications

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“…For example, a number of constitutive and inducible KB-binding proteins have recently been described, Most but not all appear to be homologous to re/ [32,33]. Furthermore, we have recently identified a constitutive 65 kDa KB-binding phosphoprotein that is closely associated with an inducible serine/threonine kinase(s) [34].…”

Section: Resultsmentioning

confidence: 97%

Herbimycin A blocks IL‐1‐induced NF‐κB DNA‐binding activity in lymphoid cell lines

Iwasaki

Uehara²,

Graves

et al. 1992

FEBS Letters

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The mechanism by which interlcukin-lor (IL-lo) activates NF-~13 DNA-binding activity is not completely understood. While it is well established Lhat protein kinase C can activate NF-~13, neither protein kinase C nor protein kinase A appears to be critical in the induction of NF-h-B by IL-la. Since a number of growth factors signal via protein tyrosine kinusc, in this study WC examined a possible involvement of protein tyrosine kinase in the IL-la-induced NF--KB. The results showed that in the murine pre-B cell line 7Oi?/3 and in the murine T cell line EL-4 6.1 ClO.iL-1 a-induced NF-xB was associated with transient increase in protein tyrosine kinasc activity. Pre-treatment of these cell lines with herbimycin A, an inhibitor of tyrosine kinase activity. blocked the IL-la-enhanced protein tyrosine kinasc activity and the IL-la-induced NF-KB DNA-binding activity. Herbimycin A at concentrations sufficient to block IL-la-induced NF-KB did not block the phorbol l2-myristate 13-ncetare(PMA)-induced NF-KB.The data suggest that IL-la and PMA activate NF-XB by different pathways and that induction of NF-KB DNA-binding activity by IL-1 might be dependent on protein tyrosine phosphotylation.

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Section: Resultsmentioning

confidence: 97%

Herbimycin A blocks IL‐1‐induced NF‐κB DNA‐binding activity in lymphoid cell lines

Iwasaki

Uehara²,

Graves

et al. 1992

FEBS Letters

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“…It is well-established that v-Rel must bind DNA in order to transform cells: the analysis of numerous mutations within the RH domain of v-Rel shows a strict correlation between the ability of v-Rel to bind DNA (and/or form dimers) and to transform cells (Ballard et al, 1990;Kumar et al, 1992;Morrison et al, 1992;Mosialos and Gilmore, 1993;Mosialos et al, 1991;White and Gilmore, 1993;Walker et al, 1992). To cite one convincing example, several mutations within the RH domain that lessen, but do not abolish, the ability of v-Rel to bind DNA, correspondingly lessen its ability to transform cells (Mosialos and Gilmore, 1993;Mosialos et al, 1991).…”

Section: Dna Binding By V-relmentioning

confidence: 99%

Multiple mutations contribute to the oncogenicity of the retroviral oncoprotein v-Rel

1999

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The avian Rev-T retrovirus encodes the v-Rel oncoprotein, which is a member of the Rel/NF-kB transcription factor family. v-Rel induces a rapidly fatal lymphoma/ leukemia in young birds, and v-Rel can transform and immortalize a variety of avian cell types in vitro. Although Rel/NF-kB transcription factors have been associated with oncogenesis in mammals, v-Rel is the only member of this family that is frankly oncogenic in animal model systems. The potent oncogenicity of v-Rel is the consequence of a number of mutations that have altered its activity and regulation: for example, certain mutations decrease its ability to be regulated by IkBa, change its DNA-binding site speci®city, and endow it with new transactivation properties. The study of v-Rel will continue to increase our knowledge of how cellular Rel proteins contribute to oncogenesis by a ecting cell growth, altering cell-cycle regulation, and blocking apoptosis. This review will discuss biological and molecular activities of v-Rel, with particular attention to how these activities relate to structure ± function aspects of the Rel/NF-kB transcription factors.

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“…Total cell lysates were prepared in lysis buffer containing 50 mM HEPES (pH 7.5) (Invitrogen Life Technologies), 5% glycerol (Invitrogen Life Technologies), 1% Triton X-100 (Sigma-Aldrich), 1 mM sodium orthovanadate (Sigma-Aldrich), 100 mM sodium chloride (Sigma-Aldrich), and protease inhibitors (Roche Applied Science). Cytoplasmic and nuclear extracts were separated as previously described (29,30). Total protein loaded was verified by BCA assay (Pierce).…”

Section: Immunoblottingmentioning

confidence: 99%

Impaired Intracellular Calcium Mobilization and NFATc1 Availability in Tolerant Anti-Insulin B Cells

Acevedo-Suárez

Kilkenny

Reich³

et al. 2006

The Journal of Immunology

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B lymphocytes that recognize soluble self-Ags are routinely found in normal individuals in a functionally inactive or anergic state. Current models indicate that this tolerant state is maintained by interactions with self-Ags that uncouple the BCR from downstream signaling pathways and increase levels of free calcium. Contrary to this expectation, B cells that harbor anti-insulin Ig transgenes (125Tg) are maintained in a tolerant state even though free calcium levels remain normal and tyrosine kinase substrate phosphorylation is preserved following BCR stimulation. Under basal conditions, intracellular levels of inositol 1,4,5-trisphosphate are increased and NFATc1 levels are reduced in 125Tg B cells. The 125Tg B cells are markedly impaired in their ability to mobilize calcium upon stimulation with ionomycin, and BCR-induced calcium mobilization from internal stores is decreased. In contrast, poisoning intracellular calcium pumps with thapsigargin increases calcium mobilization in 125Tg B cells. Changes in calcium signaling are accompanied by a failure of 125Tg B cells to translocate NFATc1 into the nucleus following stimulation with either anti-IgM or ionomycin. Thus, disassociation of BCR from multiple signaling pathways is not essential for maintaining tolerance in anti-insulin 125Tg B cells. Rather, BCRs that are occupied by autologous insulin deliver signals that induce changes in intracellular calcium mobilization and maintain tolerance by preventing activation of key transcription factors such as NFAT.

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The v-rel oncogene encodes a κB enhancer binding protein that inhibits NF-κB function

Cited by 313 publications

References 42 publications

Herbimycin A blocks IL‐1‐induced NF‐κB DNA‐binding activity in lymphoid cell lines

Herbimycin A blocks IL‐1‐induced NF‐κB DNA‐binding activity in lymphoid cell lines

Multiple mutations contribute to the oncogenicity of the retroviral oncoprotein v-Rel

Impaired Intracellular Calcium Mobilization and NFATc1 Availability in Tolerant Anti-Insulin B Cells

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