A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis

Andrew S. Venteicher, Eladio B. Abreu, Zhaojing Meng, Kelly E. McCann, Rebecca M. Terns, Timothy D. Veenstra, Michael P. Terns, Steven E. Artandi

Research output: Contribution to journalArticlepeer-review

348 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)644-648
Number of pages5
JournalScience
Volume323
Issue number5914
DOIs
StatePublished - Jan 30 2009
Externally publishedYes

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