Evidence map›Paper›PMID 15467733›Full record

ArticleOncogene2004

TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3.

Erez Perry, Rachel Tsruya, Pavel Levitsky, Oz Pomp, Michal Taller, Shira Weisberg, Wendy Parris, Sarang Kulkarni, Hana Malovani, Tony Pawson and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

28 citing papers in PubMed, 53 citations in OpenAlex.

  1. Journal of gastrointestinal oncology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Golgi Structure and Function in Health, Stress, and Diseases.Results and problems in cell differentiation · 2019
    Review
  10. STAT3 Interactors as Potential Therapeutic Targets for Cancer Treatment.International journal of molecular sciences · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

12 authors at 4 institutions in 2 countries.

Erez PerryFaculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52900, Israel.
Rachel Tsruya
Pavel Levitsky
Oz Pomp
Michal Taller
Shira Weisberg
Wendy Parris
Sarang Kulkarni
Hana Malovani
Tony Pawson
Sally Shpungin
Uri Nir
Bar-Ilan University · ILLunenfeld-Tanenbaum Research Institute · CAMount Sinai Hospital · CARabin Medical Center · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TMF/ARA160 is a Golgi resident protein whose cellular functions have not been conclusively revealed. Herein we show that TMF/ARA160 can direct the proteasomal degradation of the key cell growth regulator - Stat3. TMF/ARA160 was dispersed in the cytoplasm of myogenic C2C12 cells that were grown under low-serum conditions. The cytoplasmic distribution of TMF/ARA160 was accompanied by its transient association with the tyrosine kinase Fer and with Stat3, which underwent proteasomal degradation under those conditions. Moreover, serum deprivation induced the association of ubiquitinated proteins, with the TMF/ARA160 complex. However, TMF/ARA160 did not bind Stat1, whose cellular levels were increased in serum-starved C2C12 cells. Amino-acid sequence analysis identified a BC-box element in TMF/ARA160 that mediated the binding of this protein to elongin C. Ectopic expression of TMF/ARA160 in serum-starved C2C12 cells drove the ubiquitination and proteasomal degradation of Stat3, an effect that was not caused by TMF/ARA160 devoid of the BC-box motif. Thus, the Golgi apparatus harbors a novel BC-box-containing protein that can direct Stat3 to proteasomal degradation. Interestingly, the level of TMF/ARA160 was significantly decreased in malignant brain tumors, implying a suppressive role of that protein in tumor progression.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsBlotting, WesternBrainBrain NeoplasmsCell LineCulture Media, Serum-FreeCytoplasmDisease ProgressionDNA-Binding ProteinsDown-RegulationElonginGolgi ApparatusGolgi Matrix ProteinsImmunohistochemistryCulture Media, Serum-FreeDNA-Binding ProteinsELOC protein, humanEloc protein, mouseElonginGolgi Matrix ProteinsPhosphotyrosineProteasome Endopeptidase ComplexProtein-Tyrosine Kinasesproto-oncogene protein c-fes-fpsProto-Oncogene ProteinsStat3 protein, mouseSTAT3 Transcription FactorTMF1 protein, humanTmf1 protein, mouseTrans-ActivatorsTranscription FactorsUbiquitinUbiquitin-Protein LigasesVesicular Transport Proteins

Identifiers

PMID15467733
OpenAlexW1990707608

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.