Shelterin: the protein complex that shapes and safeguards human telomeres.

By T. de Lange. Genes & Development, 2005

3,111 citations recorded by the source corpus.

Added by telomerase, arrays of TTAGGG repeats specify the ends of human chromosomes. A complex formed by six telomere-specific proteins associates with this sequence and protects chromosome ends. By analogy to other chromosomal protein complexes such as condensin and cohesin, I will refer to this complex as shelterin. Three shelterin subunits, TRF1, TRF2, and POT1 directly recognize TTAGGG repeats. They are interconnected by three additional shelterin proteins, TIN2, TPP1, and Rap1, forming a complex that allows cells to distinguish telomeres from sites of DNA damage. Without the protective activity of shelterin, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. How does shelterin avert these events? The current data argue that shelterin is not a static structural component of the telomere. Instead, shelterin is emerging as a protein complex with DNA remodeling activity that acts together with several associated DNA repair factors to change the structure of the telomeric DNA, thereby protecting chromosome ends. Six shelterin subunits: TRF1, TRF2, TIN2, Rap1, TPP1, and POT1.

Subfields: Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/8373ec2d7dafe4603f689281ffaba3e99cf1efe0

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Citations in the corpus

Telomeres and aging. (2008, neutral): “Much progress has been made in the last decade regarding the characterization of specific proteins at telomeres and their role in telomere function (59).”
Telomerase and cancer therapeutics (2008, background): “Telomerase is the enzyme that synthesizes telomeric DNA, the terminal DNA at chromosome ends which, together with telomere-binding proteins, confers stability to chromosome”
RIF1 Is Essential for 53BP1-Dependent Nonhomologous End Joining and Suppression of DNA Double-Strand Break Resection (2013, background): “DSBs also exist at the end of all linear chromosomes but are normally protected by the telomere and its binding proteins from erroneous repair (de Lange, 2005).”
DNA methyltransferases control telomere length and telomere recombination in mammalian cells (2006, neutral): “They have an essential role in chromosome end-protection (telomere capping) and chromosomal stabilit”
Increased brood size leads to persistent eroded telomeres (2014, background): “…in “enlarged breeders” may rather reflect the inability of birds, which were forced to raise more chicks, to insure adequate telomere maintenance; mediated either by telomerase activity (Greider and Blackburn, 1985), or the pattern of expression of protecting shelterin proteins (De Lange, 2005).”
Quadruplex DNA: sequence, topology and structure (2006, neutral): “Apart from the 30 singlestranded overhang, all telomeric DNA is double-stranded [and associated with a number of telomeric proteins in the ‘shelterin’ complex (62)].”
Telomeres are favoured targets of a persistent DNA damage response in ageing and stress-induced senescence (2012, background): “Telomeres are specialized structures at the ends of linear chromosomes, and consist of tandem TTAGGG repeats that bind proteins to form a complex named shelteri”
Mechanisms of DNA damage, repair and mutagenesis (2017, positive): “…protein 2), the transcriptional repressor/activa- tor protein RAP1, and the TPP1 (POT1- and TIN2- organizing protein), which together prevent the chromosomal ends from being recognized as DNA dam- age [Takai et al., 2003; d’Adda di Fagagna et al., 2004; Liu et al., 2004; de Lange, 2005].”
Advance Publication by J-STAGE Japanese Journal of Infectious Diseases Isolation of human coronaviruses OC43, HKU1, NL63, and 229E in Yamagata, Japan, using primary human airway epithelium cells cultured by employing an air-liquid interface culture (2020, neutral): “A complex of six telomere-associated proteins (TRF1, TRF2, POT1, TIN2, TPP1, and RAP1) are known as shelterin or telosome [24] (Fig.”