Cited by 522Telomeres, Telomerase, and SenescenceNuclear Structure and FunctionRNA Research and Splicing

A Human Telomerase Holoenzyme Protein Required for Cajal Body Localization and Telomere Synthesis

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Venteicher, Andrew S., Abreu, Eladio B., Meng, Zhaojing, McCann, Kelly E., Terns, Rebecca M., Veenstra, Timothy D., Terns, Michael P., Artandi, Steven E.·2009·Science

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.

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  • TCAB1 (WDR79) is a WD40-repeat protein that binds dyskerin and the CAB box in scaRNAs.

    “TCAB1 (also known as WDR79) is a WD40-repeat containing protein that associates with dyskerin and binds the CAB box in scaRNAs (46,47).”

    From Telomeres and telomerase in cancer (2010) · cites this paper as [46]

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Authors
Venteicher, A. S., Abreu, E. B., Meng, Z., McCann, K. E., Terns, R. M., Veenstra, T. D., Terns, M. P., & Artandi, S. E.
Affiliations
Leidos (United States) (US)
Corresponding author
  • Abreu, Eladio B.
  • Meng, Zhaojing
  • Artandi, Steven E.
Venue
Science
Published
2009-01-30
Volume
323
Issue
5914
Pages
644-648
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2014414194
Cited by
522
References
23
Citations by year
2026: 13 · 2025: 16 · 2024: 20 · 2023: 18 · 2022: 22 · 2021: 30 · 2020: 29 · 2019: 27 · 2018: 28 · 2017: 29 · 2016: 43 · 2015: 39 · 2014: 40 · 2013: 37 · 2012: 35
FWCI
29.03
Type
journal article
Language
en
Open access
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • DigitalCommons-Cedarville (Cedarville University) (submittedVersion)
Funders
  • National Institutes of Health (n01co12400-79-0-22)
  • National Cancer Institute (N01CO12400, CA111691, N01-CO-012400, R01CA125453, CA125453, R01CA111691, CA104676, R01CA104676)
  • National Institute of General Medical Sciences (T32GM007365, GM 07365)
Topics
  • Health Sciences › Medicine › Physiology › Telomeres, Telomerase, and Senescence
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Keywords
telomerase, telomerase holoenzyme, Cajal bodies, telomere synthesis, dyskerin, ribonucleoprotein complexes, cancer cells
MeSH terms
Amino Acid Sequence, HeLa Cells, Humans, Molecular Sequence Data, Nuclear Proteins, RNA, Telomere, Cell Cycle Proteins, Molecular Chaperones, Telomerase, Coiled Bodies, RNA Interference, Cell Line, Tumor, Immunoprecipitation

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