MSc Thesis Defense: Büşra Kuloğlu, CHARACTERIZING THE NON-CANONICAL ACTIVITY OF ANDROGEN RECEPTOR IN PROSTATE CANCER, Date & Time: 14 July, 2026 – 10:00 AM, Place: FENS L029

CHARACTERIZING THE NON-CANONICAL ACTIVITY OF ANDROGEN

RECEPTOR IN PROSTATE CANCER

Büşra Kuloğlu
Molecular Biology, Genetics and Bioengineering, MSc Thesis, 2026

Thesis Jury

     Asst. Prof. Duygu Kuzuoğlu Öztürk (Thesis Advisor)

  Prof. Levent Öztürk

  Assoc. Prof. İbrahim Yaman

Date & Time: 14th, July 2026 – 10.00 AM

Place: FENS L029

Keywords : Androgen Receptor, RNA-Binding Proteins, Transcription Factors,

EMSA, Prostate Cancer

Abstract

Prostate cancer is the most commonly diagnosed cancer in men worldwide with high mortality. Its progression is driven by the Androgen Receptor, a transcription factor which has intrinsic DNA-binding activity. Current treatment strategies target Androgen Receptor’s ligand-binding domain to shut down this canonical signaling axis. But resistant tumors often express AR-v7 splice variant which lacks this domain entirely. AR-v7 drives a more aggressive cancer progression and immune to available treatments. Recent studies revealed that a large portion of transcription factors, including oncoproteins MYC and Estrogen-receptor-α, can also bind RNA. Whether AR shares this dual binding capacity is unknown. Here we show that endogenous AR and AR-v7 physically associate with mature RNA in prostate cancer cells. Using UV-crosslinking and RNA pulldown in 22Rv1 cells, we detected both full-length AR and AR-v7 within the bound RNA fraction, indicating that this non-canonical activity exists even in the treatment-resistant variant. We established mammalian expression systems to investigate the molecular basis of this interaction with recombinant AR protein. We then conducted cell-free binding assays with fluorescently labeled transcripts, providing a foundation for future biochemical characterization. We further generated stable cell lines expressing full-length and domain-truncated AR to map which structural regions drive this RNA interaction. Together, these findings identify AR as a candidate RNA-binding transcription factor and establish a framework for characterizing this activity across its structural domains.