The Role of Steroid Receptor Coactivator-1 in Breast Cancer

1999 ◽  
Author(s):  
Neil J. McKenna
Keyword(s):  
Breast Cancer ◽  
Steroid Receptor ◽  
Steroid Receptor Coactivator

scholarly journals SRC-3, a Steroid Receptor Coactivator: Implication in Cancer

2021 ◽  
Vol 22 (9) ◽  
pp. 4760
Author(s):  
Licen Li ◽  
Chu-Xia Deng ◽  
Qiang Chen
Keyword(s):  
Breast Cancer ◽  
Transcription Factors ◽  
Cancer Therapy ◽  
Nuclear Receptors ◽  
Essential Role ◽  
Transcriptional Activity ◽  
Steroid Receptor ◽  
Steroid Receptor Coactivator ◽  
Important Progress

Steroid receptor coactivator-3 (SRC-3), also known as amplified in breast cancer 1 (AIB1), is a member of the SRC family. SRC-3 regulates not only the transcriptional activity of nuclear receptors but also many other transcription factors. Besides the essential role of SRC-3 in physiological functions, it also acts as an oncogene to promote multiple aspects of cancer. This review updates the important progress of SRC-3 in carcinogenesis and summarizes its mode of action, which provides clues for cancer therapy.

scholarly journals Tyrosine Phosphorylation of the Nuclear Receptor Coactivator AIB1/SRC-3 Is Enhanced by Abl Kinase and Is Required for Its Activity in Cancer Cells

2008 ◽  
Vol 28 (21) ◽  
pp. 6580-6593 ◽  
Author(s):  
Annabell S. Oh ◽  
John T. Lahusen ◽  
Christopher D. Chien ◽  
Mark P. Fereshteh ◽  
Xiaolong Zhang ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Growth Factor ◽  
Cancer Cells ◽  
Tyrosine Phosphorylation ◽  
Critical Role ◽  
Steroid Receptor ◽  
Viral Oncogene ◽  
Steroid Receptor Coactivator ◽  
Abl Kinase ◽  
Viral Oncogene Homolog

ABSTRACT Overexpression and activation of the steroid receptor coactivator amplified in breast cancer 1 (AIB1)/steroid receptor coactivator-3 (SRC-3) have been shown to have a critical role in oncogenesis and are required for both steroid and growth factor signaling in epithelial tumors. Here, we report a new mechanism for activation of SRC coactivators. We demonstrate regulated tyrosine phosphorylation of AIB1/SRC-3 at a C-terminal tyrosine residue (Y1357) that is phosphorylated after insulin-like growth factor 1, epidermal growth factor, or estrogen treatment of breast cancer cells. Phosphorylated Y1357 is increased in HER2/neu (v-erb-b2 erythroblastic leukemia viral oncogene homolog 2) mammary tumor epithelia and is required to modulate AIB1/SRC-3 coactivation of estrogen receptor alpha (ERα), progesterone receptor B, NF-κB, and AP-1-dependent promoters. c-Abl (v-Abl Abelson murine leukemia viral oncogene homolog 1) tyrosine kinase directly phosphorylates AIB1/SRC-3 at Y1357 and modulates the association of AIB1 with c-Abl, ERα, the transcriptional cofactor p300, and the methyltransferase coactivator-associated arginine methyltransferase 1, CARM1. AIB1/SRC-3-dependent transcription and phenotypic changes, such as cell growth and focus formation, can be reversed by an Abl kinase inhibitor, imatinib. Thus, the phosphorylation state of Y1357 can function as a molecular on/off switch and facilitates the cross talk between hormone, growth factor, and intracellular kinase signaling pathways in cancer.

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