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

@article{citeulike:970584, abstract = {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.}, address = {The Rockefeller University, New York, New York 10021, USA. delange@mail.rockfeller.edu}, author = {de Lange, T.}, citeulike-article-id = {970584}, citeulike-linkout-0 = {http://dx.doi.org/10.1101/gad.1346005}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16166375}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16166375}, day = {15}, doi = {10.1101/gad.1346005}, issn = {0890-9369}, journal = {Genes Dev}, keywords = {capping, shelterin}, month = {September}, number = {18}, pages = {2100--2110}, posted-at = {2007-03-25 21:45:26}, priority = {2}, title = {Shelterin: the protein complex that shapes and safeguards human telomeres.}, url = {http://dx.doi.org/10.1101/gad.1346005}, volume = {19}, year = {2005} }

TY - JOUR ID - citeulike:970584 L3 - citeulike-article-id:970584 N2 - 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. IS - 18 JF - Genes Dev SN - 0890-9369 AD - The Rockefeller University, New York, New York 10021, USA. delange@mail.rockfeller.edu EP - 2110 TI - Shelterin: the protein complex that shapes and safeguards human telomeres. VL - 19 SP - 2100 KW - capping KW - shelterin AU - de Lange, T PY - 2005/09/15/ UR - http://dx.doi.org/10.1101/gad.1346005 ER -