title: A popular engagement at the ends.
abstract: Three recent studies converged on a specific protein-protein interface between TPP1 and telomerase as being crucial for the regulation of both telomerase recruitment and processivity in mammalian cells. An equivalent interaction appears to exist in budding yeast, making this a nearly universal means of telomerase regulation.
authors.affiliation: Department of Microbiology and Immunology, W.R. Hearst Microbiology Research Center, Weill Medical College of Cornell University, New York, New York, USA. nflue@med.cornell.edu
authors.forename: Neal F
authors.initials: NF
authors.lastname: Lue
authors.forename: Eun Young
authors.initials: EY
authors.lastname: Yu
authors.forename: Ming
authors.initials: M
authors.lastname: Lei
mesh_terms: D000818:Animals; D017510:Protein Folding; D034622:RNA Interference; D034741:RNA, Small Interfering; D012568:Schizosaccharomyces / Q000201:enzymology / Q000235:genetics; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry / Q000378:metabolism*; D000089804:Shelterin Complex; D019098:Telomerase / Q000737:chemistry / Q000378:metabolism*; D034501:Telomere-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D034741:RNA, Small Interfering; D029702:Schizosaccharomyces pombe Proteins; D000089804:Shelterin Complex; D034501:Telomere-Binding Proteins; C499082:pot1 protein, S pombe; D019098:Telomerase