Evidence map›Paper›PMID 9858554›Full record

ArticleMolecular and cellular biology1999

Mapping of a serine-rich domain essential for the transcriptional, antiapoptotic, and transforming activities of the v-Rel oncoprotein.

C Chen, F Agnès, C Gélinas

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Structural properties of the HNF-1A transactivation domain.Frontiers in molecular biosciences · 2023
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Stimulation of c-Rel transcriptional activity by PKA catalytic subunit beta.Journal of molecular medicine (Berlin, Germany) · 2004
    Article
  8. Article
  9. Article
  10. Article
  11. NF-kappaB in pancreatic cancer.International journal of gastrointestinal cancer · 2003
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

C ChenCenter for Advanced Biotechnology and Medicine, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854-5638, USA.
F Agnès
C Gélinas
Advanced Pharma · USRutgers, The State University of New Jersey · US

Funding

TRANS-ACTING FUNCTION OF THE V- AND C-REL ONCOPROTEINSR01CA054999 · NCI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI GELINAS, CELINE · 1996 to 2005
$1.6M
TRANS-ACTING FUNCTION OF THE V- AND C-REL ONCOPROTEINSR29CA054999 · NCI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI GELINAS, CELINE · 1991 to 1995
–
NCI NIH HHS CA-54999NCI NIH HHS R01 CA054999
6 · The paper itself

Abstract

The v-Rel oncoprotein belongs to the Rel/NF-kappaB family of transcription factors and induces aggressive lymphomas in chickens and transgenic mice. Current models for cell transformation by v-Rel invoke the combined activation of gene expression and the dominant inhibition of transcription mediated by its cellular homologs. Here, we mapped a serine-rich transactivation domain in the C terminus of v-Rel that is necessary for its biological activity. Specific serine-to-alanine substitutions within this region impaired the transcriptional activity of v-Rel, whereas a double mutant abolished its function. In contrast, substitutions with phosphomimetic aspartate residues led to a complete recovery of the transcriptional potential. The transforming activity of v-Rel mutants correlated with their ability to inhibit programmed cell death. The transforming and antiapoptotic activities of v-Rel were abolished by defined Ser-to-Ala mutations and restored by most Ser-to-Asp substitutions. However, one Ser-to-Asp mutant showed wild-type transactivation ability but failed to block apoptosis and to transform cells. These results show that the transactivation function of v-Rel is necessary but not sufficient for cell transformation, adding an important dimension to the transformation model. It is possible that defined protein-protein interactions are also required to block apoptosis and transform cells. Since v-Rel is an acutely oncogenic member of the Rel/NF-kappaB family, our data raise the possibility that phosphorylation of its serine-rich transactivation domain may regulate its unique biological activity.

Indexed as

ApoptosisCell Transformation, NeoplasticSerineTranscription, GeneticAmino Acid SequenceAnimalsAspartic AcidBinding SitesChickensCOS CellsHeLa CellsHumansMolecular Sequence DataMutagenesisOncogene Proteins v-relProto-Oncogene ProteinsAspartic AcidOncogene Proteins v-relProto-Oncogene ProteinsProto-Oncogene Proteins c-relRetroviridae Proteins, OncogenicSerine

Identifiers

PMID9858554
PMCPMC83888
OpenAlexW2156883117

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.