Shelterin
Shelterin (also called telosome) is a protein complex known to protect mammalian telomeres from DNA repair mechanisms, as well as regulate telomerase activity. In mammals and other eukaryotes, telomeric DNA consists of double- and single-stranded TTAGGG repeats and a single-stranded, G-rich overhang. Subunits of shelterin bind to these regions and induce the formation of a t-loop, a cap structure that deters DNA-damage-sensing machinery from mistakenly repairing telomeres. The absence of shelterin causes telomere uncapping and thereby activates damage-signaling pathways that may lead to non-homologous end joining (NHEJ), homology directed repair (HDR),senescence, or apoptosis.
Subunits
Shelterin has six subunits: TRF1, TRF2, POT1, RAP1, TIN2, and TPP1. They can operate in smaller subsets to regulate the length of or protect telomeres.
TRF1 (Telomere Repeat Factor 1): TRF1 is a homodimeric protein that binds to the double-stranded TTAGGG region of the telomere. It may recruit PINX1 to inhibit telomere elongation by telomerase.