A naturally occurring truncated form of FosB that inhibits Fos/Jun transcriptional activity

@article{Nakabeppu1991ANO,
  title={A naturally occurring truncated form of FosB that inhibits Fos/Jun transcriptional activity},
  author={Yusaku Nakabeppu and Daniel Nathans},
  journal={Cell},
  year={1991},
  volume={64},
  pages={751-759}
}
Both products of the fosB gene, FosB and its short form, FosB/SF, are transcriptional activators in fibroblasts.
TLDR
Constitutive expression of high levels of FosB/SF in NIH 3T3 cells has no significant inhibitory effect in the induction of cell proliferation or cell cycle progression, indicating that Fos B/SF is not a negative regulator of cell growth.
Both products of the fosB gene, FosB and its short form, FosB/SF, are transcriptional activators in fibroblasts
TLDR
Constitutive expression of high levels of FosB/SF in NIH 3T3 cells has no significant inhibitory effect in the induction of cell proliferation or cell cycle progression, indicating that Fos B/SF is not a negative regulator of cell growth.
Transcriptional regulation by Fos and Jun in vitro: interaction among multiple activator and regulatory domains
TLDR
Records show that transcriptional regulation by the Fos-Jun heterodimer results from a complex integration of multiple activator and regulatory domains, and potentially, the inhibitory domains could serve a regulatory function in vivo.
Proto-oncogene FosB: the amino terminus encodes a regulatory function required for transformation
TLDR
It is reported that transformation by FosB also requires an intact DNA-binding domain composed of the functionally bipartite basic region and leucine zipper as well as sequences present in the N terminus that serve a regulatory function.
Alternative splicing of fosB transcripts results in differentially expressed mRNAs encoding functionally antagonistic proteins.
TLDR
It is shown that serum-stimulated fibroblasts transiently express two different forms of fosB mRNA, which are generated by alternative splicing of the transcript from a single gene, indicating a new mechanisms regulating the action of members of the Fos family.
Transcriptional activation and transformation by FosB protein require phosphorylation of the carboxyl-terminal activation domain
TLDR
The results show that transcriptional activation and neoplastic transformation by the FosB protein are dependent on phosphorylation within the C terminus, and this form of control may provide a potential mechanism of signal integration at the level of a single transcription factor.
Proliferative activation of quiescent Rat-1A cells by delta FosB
TLDR
It is concluded that the N-terminal region and the DNA binding domain of FosB or delta Fos B itself have the potential to regulate cell proliferation and that the transactivation function carried by the C-terminals of FOSB is not essential for the proliferative activation of quiescent cells.
Transformation by Fos proteins requires a C-terminal transactivation domain
TLDR
It is demonstrated here that all transforming members have a C-terminal transactivation domain that is lacking in nontransforming members, and it is suggested that the subunit composition of AP1 complexes is an important determinant of mitogenic signalling capability.
The bZIP domains of Fos and Jun mediate a physical association with the TATA box-binding protein.
TLDR
It is proposed that c-Fos and c-Jun proteins function as transcriptional activators, in part by recruiting TBP to form complexes to initiate RNA synthesis.
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The product of a novel growth factor activated gene, fos B, interacts with JUN proteins enhancing their DNA binding activity.
TLDR
Immunoprecipitation studies showed that fos B as c‐fos protein, forms a complex in vitro with c‐jun and jun B proteins in the absence of a target binding sequence, suggesting thatfos B protein plays a role in control of gene expression.
Transcriptional activation and repression by Fos are independent functions: the C terminus represses immediate-early gene expression via CArG elements.
TLDR
Fos is a transcriptional regulator that can activate or repress gene expression by way of two separate functional domains that act on distinct regulatory elements.
Fos and Jun bind cooperatively to the AP-1 site: reconstitution in vitro.
TLDR
Reconstituted protein-protein and protein-DNA interactions in vitro using Fos and Jun synthesized in reticulocyte lysates demonstrate a cooperative interaction between the protein products of two proto-oncogenes with a DNA element involved in transcriptional regulation.
Fos-associated protein p39 is the product of the jun proto-oncogene.
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The products of two protooncogenes (and several related proteins), induced by extracellular stimuli, form a complex that associates with transcriptional control elements containing AP-1 sites, thereby potentially mediating the long-term responses to signals that regulate growth control and development.
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TLDR
Cl cloning and analysis of a cDNA encoding a third member of the murine jun family, jun-D, are reported here, which appears to be regulated differently than c-jun and jun-B.
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