Evidence map›Paper›PMID 23086937›Full record

ArticleThe Journal of biological chemistry2012

The F-box protein FBXO44 mediates BRCA1 ubiquitination and degradation.

Yunzhe Lu, Jiezhi Li, Dongmei Cheng, Balaji Parameswaran, Shaohua Zhang, Zefei Jiang, P Renee Yew, Junmin Peng, Qinong Ye, Yanfen Hu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

47 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. BARD1: A Friend or Foe in Pancreatic Ductal Adenocarcinoma?International journal of molecular sciences · 2025
    Review
  11. Article
  12. Review
  13. SKP1-CUL1-F-box: Key molecular targets affecting disease progression.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  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

10 authors at 3 institutions in 2 countries.

Yunzhe LuDepartment of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78229, USA.
Jiezhi Li
Dongmei Cheng
Balaji Parameswaran
Shaohua Zhang
Zefei Jiang
P Renee Yew
Junmin Peng
Qinong Ye
Yanfen Hu
The University of Texas Health Science Center at San Antonio · USAcademy of Military Medical Sciences · CNEmory University · US

Funding

TISSUE CULTURE---COREP30CA054174 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI DARUKA MAHADEVAN · 1991 to 2026
$59.1M
The Mechanism of BRCA1 in Tumor SuppressionR01CA118578 · NCI · UNIVERSITY OF VIRGINIA · PI HU, YANFEN · 2006 to 2010
$1.1M
NCI NIH HHS P30 CA054174NCI NIH HHS P30CA054174NCI NIH HHS R01 CA118578NCI NIH HHS R01CA118578
6 · The paper itself

Abstract

BRCA1 mutations account for a significant proportion of familial breast and ovarian cancers. In addition, reduced BRCA1 protein is associated with sporadic cancer cases in these tissues. At the cellular level, BRCA1 plays a critical role in multiple cellular functions such as DNA repair and cell cycle checkpoint control. Its protein level is regulated in a cell cycle-dependent manner. However, regulation of BRCA1 protein stability is not fully understood. Our earlier study showed that the amino terminus of BRCA1 harbors a degron sequence that is sufficient and necessary for conferring BRCA1 degradation. In the current study, we used mass spectrometry to identify Skp1 that regulates BRCA1 protein stability. Small interfering RNA screening that targets all human F-box proteins uncovered FBXO44 as an important protein that influences BRCA1 protein level. The Skp1-Cul1-F-box-protein44 (SCF(FBXO44)) complex ubiquitinates full-length BRCA1 in vitro. Furthermore, the N terminus of BRCA1 mediates the interaction between BRCA1 and FBXO44. Overexpression of SCF(FBXO44) reduces BRCA1 protein level. Taken together, our work strongly suggests that SCF(FBXO44) is an E3 ubiquitin ligase responsible for BRCA1 degradation. In addition, FBXO44 expression pattern in breast carcinomas suggests that SCF(FBXO44)-mediated BRCA1 degradation might contribute to sporadic breast tumor development.

Indexed as

Gene Expression Regulation, NeoplasticBRCA1 ProteinBreast NeoplasmsCell CycleDNA RepairF-Box ProteinsFemaleHEK293 CellsHumansMass SpectrometryMutationProtein BindingProtein Structure, TertiaryRNA, Small InterferingS-Phase Kinase-Associated ProteinsUbiquitinBRCA1 ProteinBRCA1 protein, humanF-Box ProteinsFBXO44 protein, humanRNA, Small InterferingSKP1 protein, humanS-Phase Kinase-Associated ProteinsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID23086937
PMCPMC3510804
OpenAlexW2075976137

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.