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TRIM33 Is a Co-Regulator of Estrogen Receptor Alpha.
Romo, Bianca A; Karakyriakou, Barbara; Cressey, Lauren; Brauer, Brooke L; Yang, Huijuan; Warren, Alexa; Johnson, Anneka L; Kettenbach, Arminja N; Miller, Todd W.
Afiliación
  • Romo BA; Department of Molecular and Systems Biology, Geisel School of Medicine at Dartmouth, Lebanon, NH 03755, USA.
  • Karakyriakou B; Department of Molecular and Systems Biology, Geisel School of Medicine at Dartmouth, Lebanon, NH 03755, USA.
  • Cressey L; Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Lebanon, NH 03755, USA.
  • Brauer BL; Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Lebanon, NH 03755, USA.
  • Yang H; Department of Molecular and Systems Biology, Geisel School of Medicine at Dartmouth, Lebanon, NH 03755, USA.
  • Warren A; Department of Molecular and Systems Biology, Geisel School of Medicine at Dartmouth, Lebanon, NH 03755, USA.
  • Johnson AL; Department of Molecular and Systems Biology, Geisel School of Medicine at Dartmouth, Lebanon, NH 03755, USA.
  • Kettenbach AN; Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Lebanon, NH 03755, USA.
  • Miller TW; Department of Molecular and Systems Biology, Geisel School of Medicine at Dartmouth, Lebanon, NH 03755, USA.
Cancers (Basel) ; 16(5)2024 Feb 20.
Article en En | MEDLINE | ID: mdl-38473207
ABSTRACT
Estrogen receptor alpha (ER)-positive breast cancer is responsible for over 60% of breast cancer cases in the U.S. Among patients diagnosed with early-stage ER+ disease, 1/3 will experience recurrence despite treatment with adjuvant endocrine therapy. ER is a nuclear hormone receptor responsible for estrogen-driven tumor growth. ER transcriptional activity is modulated by interactions with coregulators. Dysregulation of the levels of these coregulators is involved in the development of endocrine resistance. To identify ER interactors that modulate transcriptional activity in breast cancer, we utilized biotin ligase proximity profiling of ER interactomes. Mass spectrometry analysis revealed tripartite motif containing 33 (TRIM33) as an estrogen-dependent interactor of ER. shRNA knockdown showed that TRIM33 promoted ER transcriptional activity and estrogen-induced cell growth. Despite its known role as an E3 ubiquitin ligase, TRIM33 increased the stability of endogenous ER in breast cancer cells. TRIM33 offers a novel target for inhibiting estrogen-induced cancer cell growth, particularly in cases of endocrine resistance driven by ER (ESR1) gene amplification or overexpression.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Cancers (Basel) Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Suiza
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Cancers (Basel) Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Suiza