Telomeric repeat-binding factor 1 (TERF1)

Telomeric Repeat-binding Factor 1 (TERF1), also known as TRF1, is a crucial component of the shelterin complex, a specialized multiprotein complex that protects the ends of chromosomes (telomeres) in mammalian cells. TERF1 directly binds to the TTAGGG telomeric DNA repeats. Its primary biological functions include regulating telomere length by inhibiting telomerase, protecting chromosome ends from being recognized as DNA damage, facilitating efficient replication through telomeric regions, and organizing telomeric chromatin structure. Deregulation, particularly overexpression, of TERF1 has been implicated in the development and progression of various cancers, where it contributes to sustained proliferation and survival of malignant cells, making it an attractive therapeutic target for cancer treatment.

Other names

TRF1TRFPIN2TRBF1hTRF1-ASt-TRF1telomeric repeat-binding factor (NIMA-interacting) 1TTAGGG repeat-binding factor 1NIMA-interacting protein 2

Drugs targeting TERF1 typically aim to disrupt its binding to telomeric DNA, interfere with its protein-protein interactions within the shelterin complex, or promote its degradation. This leads to telomere deprotection, increased telomere shortening, activation of DNA damage responses at telomeres, and induction of cellular senescence or apoptosis in cancer cells, thereby inhibiting tumor growth.