The leucine repeat motif in Fos protein mediates complex formation with Jun/AP-1 and is required for transformation

Schuermann, Marcus; Neuberg, Manfred; Hunter, John B.; Jenuwein, Thomas; Ryseck, Rolf-Peter; Bravo, Rodrigo; Müller, Rolf

doi:10.1016/0092-8674(89)90253-5

Cited by 282 publications

(149 citation statements)

References 32 publications

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“…Residues at e and g positions seem to be less important. In general, our predictions are in agreement with experiment (Schuermann et al, 1989(Schuermann et al, , 1991O'Shea et al, 1992); however, further investigation is required to determine the specific role of any given residue in the preferential heterodimer formation. Because preferential heterodimer formation results from the relative instability of Fos homodimers, all of the residues responsible for the relative instability of Fos homodimers ultimately drive the process of heterodimerization.…”

Section: Discussionsupporting

confidence: 85%

Method for Predicting the State of Association of Discretized Protein Models. Application to Leucine Zippers^†

1996

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A method that employs a transfer matrix treatment combined with Monte Carlo sampling has been used to calculate the configurational free energies of folded and unfolded states of lattice models of proteins. The method is successfully applied to study the monomer-dimer equilibria in various coiled coils. For the short coiled coils, GCN4 leucine zipper, and its fragments, Fos and Jun, very good agreement is found with experiment. Experimentally, some subdomains of the GCN4 leucine zipper form stable dimeric structures, suggesting the regions of differential stability in the parent structure. Our calculations suggest that the stabilities of the subdomains are in general different from the values expected simply from the stability of the corresponding fragment in the wild type molecule. Furthermore, parts of the fragments structurally rearrange in some regions with respect to their corresponding wild type positions. Our results suggest for an Asn in the dimerization interface at least a pair of hydrophobic interacting helical turns at each side is required to stabilize the stable coiled coil. Finally, the specificity of heterodimer formation in the Fos-Jun system comes from the relative instability of Fos homodimers, resulting from unfavorable intra-and interhelical interactions in the interfacial coiled coil region.

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Section: Discussionsupporting

confidence: 85%

Method for Predicting the State of Association of Discretized Protein Models. Application to Leucine Zippers^†

1996

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“…c-Fos expressed in a coupled transcription/translation system is phosphorylated [29,30]. Indeed, the inclusion of [7-32P] -ATP in the translation mixture yielded labeled protein (data not shown).…”

Section: C-fos Is Taken Up In Vitro By Freshly Isolated Lysosomesmentioning

confidence: 94%

“…A plasmid that contained a rat cDNA encoding the wild-type c-Fos [29] or pTZE300 encoding vFos [30] was transcribed (after linearization with HindlII), essentially as suggested by the supplier, with either SP6 (c-Fos) or T7 (v-Fos) RNA polymerases (Promega). The resulting mRNAs (from 6 gg of template DNA) were used in a translation reaction (50 p-l) that contained nuclease-treated rabbit reticulocyte lysate (40 p.1; Promega) in the presence of 6 p-I of L-[35S]methionine (> 1000 Ci/mmol; Amersham).…”

Section: F Aniento Et Alifebs Letters 390 (1996) 47-52mentioning

confidence: 99%

“…1B, v-Fos was incorporated into lysosomes, albeit ~3 times less efficiently than c-Fos (Table 1). It should be noted that the two bands observed for v-Fos are always generated by in vitro transcription/translation of the v-Fos encoding construct pTZE300 [30,31], most likely the faster migrating species representing leakage in either of these processes.…”

Section: C-fos Is Taken Up In Vitro By Freshly Isolated Lysosomesmentioning

confidence: 99%

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Selective uptake and degradation of c‐Fos and v‐Fos by rat liver lysosomes

et al. 1996

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The transcription factor c-Fos is a short-lived protein and calpains and uhiquitin-dependent systems have been proposed to be involved in its degradation. In this report, we consider a lysosomal degradation pathway for c-Fos. Using a cell-free assay, we have found that freshly isolated lysosomes can take up and degrade c-Fos with high efficiency, v-Fos, the oncogenic counterpart of c-Fos, can also be taken up by lysosomes, yet the amount of incorporated protein is much lower, c-Fos uptake is independent of its phosphorylation state but it appears to be regulated by dimerization with differentially phosphorylated forms of c-Jun, while v-Fos escapes this regulation. Moreover, we show that c-Fos is immunologically detected in lysosomes isolated from the fiver of rats treated with the protease inhibitor leupeptin. Altogether, these results suggest that lysosomes can also participate in the selective degradation of c-Fos in rat liver.

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“…Two activator plasmids expressing a hybrid v-fos oncogene (pGY-FOS; Schuermann et al, 1989) or the mouse c-jun proto-oncogene (pGY-JUN; Ryseck et al, 1988) were added together with the reporter plasmids. These cotransfections resulted in a dramatic stimulation of the chimeric promoters harboring the B consensus [ Figure 2; plxB-MIC to p5xB-MIC (lanes 8 to 12) compared with pMlC (lane 7)].…”

Section: Fos and Jun Transactivate Chimeric Promoters Containing One mentioning

confidence: 99%

Fos and Jun oncogenes transactivate chimeric or native promoters containing AP1/GCN4 binding sites in plant cells.

et al. 1990

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The function of mammalian transcription factors of the leucine zipper class was investigated in leaf-derived protoplasts of tobacco. In transient expression experiments, Fos and Jun strongly activated chimeric promoters composed of the TATA box region of the cauliflower mosaic virus 35s transcript preceded by one to five copies of an APl/GCN4 binding site. Fos and Jun also stimulated a wheat high molecular weight glutenin promoter in which similar binding sites are located more than 500 base pairs from its transcription start site. Both the DNA binding and the transcription activation domains of these proteins were required for proper promoter stimulation by Fos and Jun. Each factor alone was partially active, suggesting that at least the Fos protein can associate with an endogenous plant transcription factor. These observations support the hypothesis that sequences related to APl/GCN4 binding sites could be cis-acting modules involved in the transcriptional regulation of plant genes.

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The leucine repeat motif in Fos protein mediates complex formation with Jun/AP-1 and is required for transformation

Cited by 282 publications

References 32 publications

Method for Predicting the State of Association of Discretized Protein Models. Application to Leucine Zippers^†

Method for Predicting the State of Association of Discretized Protein Models. Application to Leucine Zippers^†

Selective uptake and degradation of c‐Fos and v‐Fos by rat liver lysosomes

Fos and Jun oncogenes transactivate chimeric or native promoters containing AP1/GCN4 binding sites in plant cells.

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The leucine repeat motif in Fos protein mediates complex formation with Jun/AP-1 and is required for transformation

Cited by 282 publications

References 32 publications

Method for Predicting the State of Association of Discretized Protein Models. Application to Leucine Zippers†

Method for Predicting the State of Association of Discretized Protein Models. Application to Leucine Zippers†

Selective uptake and degradation of c‐Fos and v‐Fos by rat liver lysosomes

Fos and Jun oncogenes transactivate chimeric or native promoters containing AP1/GCN4 binding sites in plant cells.

Contact Info

Product

Resources

About

Method for Predicting the State of Association of Discretized Protein Models. Application to Leucine Zippers^†

Method for Predicting the State of Association of Discretized Protein Models. Application to Leucine Zippers^†