Evidence map›Paper›PMID 23940030›Full record

ArticleThe Journal of biological chemistry2013

The F-box protein FBXO25 promotes the proteasome-dependent degradation of ELK-1 protein.

Felipe R Teixeira, Adriana O Manfiolli, Cláudia S Soares, Munira M A Baqui, Tie Koide, Marcelo D Gomes

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

13 citing papers in PubMed, 30 citations in OpenAlex.

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  12. FBXO25 promotes cell proliferation, invasion, and migration of NSCLC.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  13. Review
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

6 authors at 1 institution in 1 country.

Felipe R TeixeiraFrom the Departments of Biochemistry and Immunology and.
Adriana O Manfiolli
Cláudia S Soares
Munira M A Baqui
Tie Koide
Marcelo D Gomes
Universidade de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FBXO25 is one of the 69 known human F-box proteins that serve as specificity factors for a family of ubiquitin ligases composed of SKP1, Rbx1, Cullin1, and F-box protein (SCF1) that are involved in targeting proteins for degradation across the ubiquitin proteasome system. However, the substrates of most SCF E3 ligases remain unknown. Here, we applied an in chip ubiquitination screen using a human protein microarray to uncover putative substrates for the FBXO25 protein. Among several novel putative targets identified, the c-fos protooncogene regulator ELK-1 was characterized as the first endogenous substrate for SCF1(FBXO25) E3 ligase. FBXO25 interacted with and mediated the ubiquitination and proteasomal degradation of ELK-1 in HEK293T cells. In addition, FBXO25 overexpression suppressed induction of two ELK-1 target genes, c-fos and egr-1, in response to phorbol 12-myristate 13-acetate. Together, our findings show that FBXO25 mediates ELK-1 degradation through the ubiquitin proteasome system and thereby plays a role in regulating the activation of ELK-1 pathway in response to mitogens.

Indexed as

Gene Expression RegulationEarly Growth Response Protein 1ets-Domain Protein Elk-1F-Box ProteinsHEK293 CellsHumansNerve Tissue ProteinsProteasome Endopeptidase ComplexProtein Array AnalysisProteolysisProteomicsProto-Oncogene Proteins c-fosTetradecanoylphorbol AcetateUbiquitinEarly Growth Response Protein 1EGR1 protein, humanELK1 protein, humanets-Domain Protein Elk-1F-Box ProteinsFBXO25 protein, humanNerve Tissue ProteinsProteasome Endopeptidase ComplexProto-Oncogene Proteins c-fosTetradecanoylphorbol AcetateUbiquitinE3 Ubiquitin Ligaseegr-1Ets Family Transcription FactorProteasomeProtein Degradation

Identifiers

PMID23940030
PMCPMC3784726
OpenAlexW2022283793

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.