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Article

JunD-menin interaction regulates c-Jun-mediated AP-1 transactivation.

Endocrine journal - 1 Jun 2004

Ikeo Yasuto, Yumita Wataru, Sakurai Akihiro, Hashizume Kiyoshi

Abstract excerpt

The gene responsible for multiple endocrine neoplasia type 1, MEN1, encodes the 610-amino acid-protein, menin. Although menin has been reported to bind AP-1 transcription factor JunD and suppress its transcriptional activity, little is known about its molecular mechanisms and physiological role. To better understand the function of menin and its significance in tumorigenesis, we investigated the effect of...

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Source

Identifiers

PMID: 15256779
DOI: 10.1507/endocrj.51.333

Genes

MEN1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

JunD-menin interaction regulates c-Jun-mediated AP-1 transactivation.PMID 15256779Read ↗

Menin represses JunD-activated transcription by a histone deacetylase-dependent mechanism.Semantic proximity Read ↗

Transcription factor JunD, deprived of menin, switches from growth suppressor to growth promoterSemantic proximity Read ↗

Genetic interactions between Drosophila melanogaster menin and Jun/Fos.Semantic proximity Read ↗

Menin Molecular Interactions: Insights into Normal Functions and TumorigenesisSemantic proximity Read ↗

Menin and JunD regulate gastrin gene expression through proximal DNA elementsSemantic proximity Read ↗

Epigenetic regulation by the menin pathwaySemantic proximity Read ↗

Menin regulates endocrine diseases by controlling histone modification and gene transcription.Semantic proximity Read ↗

Multiple endocrine neoplasia type 1.Semantic proximity Read ↗

Multi-omics analyses of MEN1 missense mutations identify disruption of menin-MLL and menin-JunD interactions as critical requirements for molecular pathogenicitySemantic proximity Read ↗

Multi-omics analyses of MEN1 missense mutations identify disruption of menin–MLL and menin–JunD interactions as critical requirements for molecular pathogenicitySemantic proximity Read ↗

Menin: the protein behind the MEN1 syndrome.Semantic proximity Read ↗

Menin in CancerSemantic proximity Read ↗

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