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. 2020 Sep 24;12(10):2739. doi: 10.3390/cancers12102739

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Shelterin complex and Protection of Telomeres 1 (POT1) protein. (A) Telomeres are composed of tandem repetitive TTAGGG sequences that are predominantly double-stranded (ds) but terminate in a single stranded (ss) 3′-overhang of the G-rich strand [6,36]. Telomeres are shielded with the shelterin complex, consisting of the TRF1, TRF2, RAP1, TIN2, TPP1 and POT1 proteins. POT1 binds to the TPP1 protein and to telomeric ss DNA through its C- and N-termini, respectively, and controls the sequence at the ds/ss junction. The human POT1 protein contains three oligonucleotide/oligosaccharide-binding (OB) fold domains, namely OB1-3, and OB3 has an embedded Holliday junction resolvase-like (HJRL) domain. (B) POT1 splice variants and their functions [21,29,37]