Evidence map›Paper›PMID 25944903›Full record

ArticleThe Journal of biological chemistry2015

FBXO32 Targets c-Myc for Proteasomal Degradation and Inhibits c-Myc Activity.

Zhichao Mei, Dawei Zhang, Bo Hu, Jing Wang, Xian Shen, Wuhan Xiao

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

46 citing papers in PubMed, 92 citations in OpenAlex.

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  5. World journal of gastroenterology · 2025
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  20. RAI14 Promotes Melanoma Progression by Regulating the FBXO32/c-MYC Pathway.International journal of molecular sciences · 2022
    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

6 authors at 3 institutions in 1 country.

Zhichao MeiFrom the Key Laboratory of Aquatic Biodiversity and Conservation and.
Dawei ZhangFrom the Key Laboratory of Aquatic Biodiversity and Conservation and.
Bo HuFrom the Key Laboratory of Aquatic Biodiversity and Conservation and.
Jing WangFrom the Key Laboratory of Aquatic Biodiversity and Conservation and.
Xian Shenthe First Hospital of Wenzhou Medical University, Wenzhou 325000, China.
Wuhan XiaoFrom the Key Laboratory of Aquatic Biodiversity and Conservation and the State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, China and w-xiao@ihb.ac.cn.
Institute of Hydrobiology · CNChinese Academy of Sciences · CNFirst Affiliated Hospital of Wenzhou Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FBXO32 (MAFbx/Atrogin-1) is an E3 ubiquitin ligase that is markedly up-regulated in muscle atrophy. Although some data indicate that FBXO32 may play an important role in tumorigenesis, the molecular mechanism of FBXO32 in tumorigenesis has been poorly understood. Here, we present evidence that FBXO32 targets the oncogenic protein c-Myc for ubiquitination and degradation through the proteasome pathway. Phosphorylation of c-Myc at Thr-58 and Ser-62 is dispensable for FBXO32 to induce c-Myc degradation. Mutation of the lysine 326 in c-Myc reduces c-Myc ubiquitination and prevents the c-Myc degradation induced by FBXO32. Furthermore, overexpression of FBXO32 suppresses c-Myc activity and inhibits cell growth, but knockdown of FBXO32 enhances c-Myc activity and promotes cell growth. Finally, we show that FBXO32 is a direct downstream target of c-Myc, highlighting a negative feedback regulation loop between c-Myc and FBXO32. Thus, FBXO32 may function by targeting c-Myc. This work explains the function of FBXO32 and highlights its mechanisms in tumorigenesis.

Indexed as

Amino Acid MotifsAnimalsCell ProliferationHumansMiceMuscle ProteinsMuscle, SkeletalMuscular AtrophyPhosphorylationProteasome Endopeptidase ComplexProtein BindingProteolysisProto-Oncogene Proteins c-mycSKP Cullin F-Box Protein LigasesUbiquitinationFBXO32 protein, humanMuscle ProteinsProteasome Endopeptidase ComplexProto-Oncogene Proteins c-mycSKP Cullin F-Box Protein Ligasescell proliferationFBXO32muscle atrophyMyc (c-Myc)oncogeneproteasomal degradationubiquitylation (ubiquitination)

Identifiers

PMID25944903
PMCPMC4481220
OpenAlexW336919607

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.