Science · 2009 · 528 citations · 19 references
Life SciencesGeneticsMolecular BiologyCancer GeneticsMolecular OncologyRna ProcessingProtein SynthesisRna InterferenceRna-protein InteractionsTelomere BiologyTelomere Biology In CancerTelomere MaintenanceAuxiliary SubunitsCajal BodiesTelomerase EnzymeTelomerase FunctionTelomerase RegulationTelomerase Reverse TranscriptaseTelomere Dna SynthesisTelomere-associated Proteins
Telomerase is a ribonucleoprotein (RNP) complex that synthesizes telomere repeats in tissue progenitor cells and cancer cells. Active human telomerase consists of at least three principal subunits, including the telomerase reverse transcriptase, the telomerase RNA (TERC), and dyskerin. Here, we identify a holoenzyme subunit, TCAB1 (telomerase Cajal body protein 1), that is notably enriched in Cajal bodies, nuclear sites of RNP processing that are important for telomerase function. TCAB1 associates with active telomerase enzyme, established telomerase components, and small Cajal body RNAs that are involved in modifying splicing RNAs. Depletion of TCAB1 by using RNA interference prevents TERC from associating with Cajal bodies, disrupts telomerase-telomere association, and abrogates telomere synthesis by telomerase. Thus, TCAB1 controls telomerase trafficking and is required for telomere synthesis in human cancer cells.
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The POT1–TPP1 telomere complex is a telomerase processivity factor
Feng Wang, Elaine R. Podell, Arthur J. Zaug et al. · Nature · 2007 · 709 citations · Full text
Protein Composition of Catalytically Active Human Telomerase from Immortal Cells
Scott B. Cohen, Mark E. Graham, George O. Lovrecz et al. · Science · 2007 · 661 citations
TPP1 is a homologue of ciliate TEBP-β and interacts with POT1 to recruit telomerase
Huawei Xin, Dan Liu, Ma Wan et al. · Nature · 2007 · 475 citations