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Updated: Feb 3, 2026

Profiling of Estrogen-regulated MicroRNAs in Breast Cancer Cells
Published on: February 21, 2014
Estrogen Receptor Alpha and its Ubiquitination in Breast Cancer Cells
Angeles C Tecalco-Cruz1, Josué O Ramírez-Jarquín2, Eduardo Cruz-Ramos1
1Instituto de Investigaciones Biomedicas. Universidad Nacional Autonoma de Mexico. Mexico City, 04510, Mexico.
Abstract:
More than 70% of all breast cancer cases are estrogen receptor alpha-positive (ERα). ERα is a member of the nuclear receptor family, and its activity is implicated in the gene transcription linked to the proliferation of breast cancer cells, as well as in extranuclear signaling pathways related to the development of resistance to endocrine therapy. Protein-protein interactions and posttranslational modifications of ERα underlie critical mechanisms that modulate its activity. In this review, the relationship between ERα and ubiquitin protein (Ub), was investigated in the context of breast cancer cells. Interestingly, Ub can bind covalently or non-covalently to ERα resulting in either a proteolytic or non-proteolytic fate for this receptor. Thereby, Ub-dependent molecular pathways that modulate ERα signaling may play a central role in breast cancer progression, and consequently, present critical targets for treatment of this disease.
Insights
Ubiquitin protein (Ub) interactions with estrogen receptor alpha (ERα) impact breast cancer cell growth and endocrine therapy resistance. Understanding these Ub-dependent pathways offers new therapeutic targets for breast cancer treatment.
Area of Science:
- Molecular Biology
- Oncology
- Biochemistry
Background:
- Estrogen receptor alpha (ERα) drives proliferation in over 70% of breast cancers.
- ERα signaling is crucial for breast cancer cell growth and endocrine therapy resistance.
- Posttranslational modifications and protein interactions regulate ERα activity.
Purpose of the Study:
- To investigate the role of ubiquitin protein (Ub) in modulating estrogen receptor alpha (ERα) activity in breast cancer.
- To explore Ub-ERα interactions in the context of breast cancer progression.
- To identify Ub-dependent pathways as potential therapeutic targets.
Main Methods:
- Literature review focusing on ubiquitin-ERα interactions.
- Analysis of molecular mechanisms governing ERα ubiquitination.
- Examination of signaling pathways affected by Ub-ERα binding.
Main Results:
- Ubiquitin can bind to ERα covalently or non-covalently.
- These interactions lead to either proteolytic degradation or non-proteolytic functional modulation of ERα.
- Ubiquitin-dependent pathways significantly influence ERα signaling in breast cancer cells.
Conclusions:
- Ubiquitin conjugation plays a critical role in regulating ERα function in breast cancer.
- Ub-ERα interactions are implicated in breast cancer progression and endocrine resistance.
- Targeting Ub-dependent pathways modulating ERα presents a promising therapeutic strategy.
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